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  • 1.
    Contardi, Cecilia
    et al.
    Department of Drug Sciences, University of Pavia, 27100 Pavia, PV, Italy.
    Rubes, Davide
    Department of Drug Sciences, University of Pavia, 27100 Pavia, PV, Italy.
    Serra, Massimo
    Department of Drug Sciences, University of Pavia, 27100 Pavia, PV, Italy.
    Dorati, Rossella
    Department of Drug Sciences, University of Pavia, 27100 Pavia, PV, Italy.
    Dattilo, Marco
    Department of Pharmacy, Health and Nutritional Sciences, University of Calabria, 87036 Arcavacata di Rende, CS, Italy.
    Mavliutova, Liliia
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Patrini, Maddalena
    Department of Physics, University of Pavia, 27100 Pavia, PV, Italy.
    Guglielmann, Raffaella
    Department of Mathematics F. Casorati, University of Pavia, 27100 Pavia, PV, Italy.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    De Lorenzi, Ersilia
    Department of Drug Sciences, University of Pavia, 27100 Pavia, PV, Italy.
    Affinity Capillary Electrophoresis as a Tool To Characterize Molecularly Imprinted Nanogels in Solution2024In: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 96, no 7, p. 3017-3024Article in journal (Refereed)
    Abstract [en]

    In this work, an innovative and accurate affinity capillary electrophoresis (ACE) method was set up to monitor the complexation of aqueous MIP nanogels (NGs) with model cancer-related antigens. Using α2,6′- and α2,3′-sialyllactose as oversimplified cancer biomarker-mimicking templates, NGs were synthesized and characterized in terms of size, polydispersity, and overall charge. A stability study was also carried out in order to select the best storage conditions and to ensure product quality. After optimization of capillary electrophoresis conditions, injection of MIP NGs resulted in a single, sharp, and efficient peak. The mobility shift approach was applied to quantitatively estimate binding affinity, in this case resulting in an association constant of K ≈ 106 M–1. The optimized polymers further displayed a pronounced discrimination between the two sialylated sugars. The newly developed ACE protocol has the potential to become a very effective method for nonconstrained affinity screening of NG in solution, especially during the NG development phase and/or for a final accurate quantitation of the observed binding.

  • 2.
    Sergeeva, Yulia
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Yeung, Sing Yee
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Heteromultivalent Ligand Display on Reversible Self-Assembled Monolayers (rSAMs): A Fluidic Platform for Tunable Influenza Virus Recognition2024In: ACS Applied Materials and Interfaces, ISSN 1944-8244, E-ISSN 1944-8252, Vol. 16, no 3, p. 3139-3146Article in journal (Refereed)
    Abstract [en]

    We report on the design of heteromultivalent influenza A virus (IAV) receptors based on reversible self-assembled monolayers (SAMs) featuring two distinct mobile ligands. The principal layer building blocks consist of α-(4-amidinophenoxy)alkanes decorated at the ω-position with sialic acid (SA) and the neuraminidase inhibitor Zanamivir (Zan), acting as two mobile ligands binding to the complementary receptors hemagglutinin (HA) and neuraminidase (NA) on the virus surface. From ternary amphiphile mixtures comprising these ligands, the amidines spontaneously self-assemble on top of carboxylic acid-terminated SAMs to form reversible mixed monolayers (rSAMs) that are easily tunable with respect to the ligand ratio. We show that this results in the ability to construct surfaces featuring a very strong affinity for the surface proteins and specific virus subtypes. Hence, an rSAM prepared from solutions containing 15% SA and 10% Zan showed an exceptionally high affinity and selectivity for the avian IAV H7N9 (Kd = 11 fM) that strongly exceeded the affinity for other subtypes (H3N2, H5N1, H1N1). Changing the SA/Zan ratio resulted in changes in the relative preference between the four tested subtypes, suggesting this to be a key parameter for rapid adjustments of both virus affinity and selectivity.

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  • 3.
    Huynh, Chau Minh
    et al.
    Department of Chemistry, Umeå University, S-90187 Umeå, Sweden.
    Mavliutova, Liliia
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Sparrman, Tobias
    Department of Chemistry, Umeå University, S-90187 Umeå, Sweden.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Irgum, Knut
    Department of Chemistry, Umeå University, S-90187 Umeå, Sweden.
    Elucidation of the Binding Orientation in α2,3- and α2,6-Linked Neu5Ac-Gal Epitopes toward a Hydrophilic Molecularly Imprinted Monolith.2023In: ACS Omega, E-ISSN 2470-1343, Vol. 8, no 46, p. 44238-44249Article in journal (Refereed)
    Abstract [en]

    N-Acetylneuraminic acid and its α2,3/α2,6-glycosidic linkages with galactose (Neu5Ac-Gal) are major carbohydrate antigen epitopes expressed in various pathological processes, such as cancer, influenza, and SARS-CoV-2. We here report a strategy for the synthesis and binding investigation of molecularly imprinted polymers (MIPs) toward α2,3 and α2,6 conformations of Neu5Ac-Gal antigens. Hydrophilic imprinted monoliths were synthesized from melamine monomer in the presence of four different templates, namely, N-acetylneuraminic acid (Neu5Ac), N-acetylneuraminic acid methyl ester (Neu5Ac-M), 3′-sialyllactose (3SL), and 6′-sialyllactose (6SL), in a tertiary solvent mixture at temperatures varying from −20 to +80 °C. The MIPs prepared at cryotemperatures showed a preferential affinity for the α2,6 linkage sequence of 6SL, with an imprinting factor of 2.21, whereas the α2,3 linkage sequence of 3SL resulted in nonspecific binding to the polymer scaffold. The preferable affinity for the α2,6 conformation of Neu5Ac-Gal was evident also when challenged by a mixture of other mono- and disaccharides in an aqueous test mixture. The use of saturation transfer difference nuclear magnetic resonance (STD-NMR) on suspensions of crushed monoliths allowed for directional interactions between the α2,3/α2,6 linkage sequences on their corresponding MIPs to be revealed. The Neu5Ac epitope, containing acetyl and polyalcohol moieties, was the major contributor to the sequence recognition for Neu5Ac(α2,6)Gal(β1,4)Glc, whereas contributions from the Gal and Glc segments were substantially lower.

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  • 4.
    Grasso, Giuliana
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces. Department of Pharmacy, University of Salerno, Via Giovanni Paolo II 132, 84084, Fisciano, SA, Italy.
    Sommella, Eduardo M
    Department of Pharmacy, University of Salerno, Via Giovanni Paolo II 132, 84084, Fisciano, SA, Italy.
    Merciai, Fabrizio
    Department of Pharmacy, University of Salerno, Via Giovanni Paolo II 132, 84084, Fisciano, SA, Italy.
    Abouhany, Rahma
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Shinde, Sudhirkumar A
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces. School of Consciousness, Dr. Vishwanath Karad MIT World Peace University, 411038, Pune, India.
    Campiglia, Pietro
    Department of Pharmacy, University of Salerno, Via Giovanni Paolo II 132, 84084, Fisciano, SA, Italy.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Crescenzi, Carlo
    Department of Pharmacy, University of Salerno, Via Giovanni Paolo II 132, 84084, Fisciano, SA, Italy.
    Enhanced selective capture of phosphomonoester lipids enabling highly sensitive detection of sphingosine 1-phosphate2023In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 415, no 26, p. 6573-6582Article in journal (Refereed)
    Abstract [en]

    Sphingolipids play crucial roles in cellular membranes, myelin stability, and signalling responses to physiological cues and stress. Among them, sphingosine 1-phosphate (S1P) has been recognized as a relevant biomarker for neurodegenerative diseases, and its analogue FTY-720 has been approved by the FDA for the treatment of relapsing-remitting multiple sclerosis. Focusing on these targets, we here report three novel polymeric capture phases for the selective extraction of the natural biomarker and its analogue drug. To enhance analytical performance, we employed different synthetic approaches using a cationic monomer and a hydrophobic copolymer of styrene-DVB. Results have demonstrated high affinity of the sorbents towards S1P and fingolimod phosphate (FTY-720-P, FP). This evidence proved that lipids containing phosphate diester moiety in their structures did not constitute obstacles for the interaction of phosphate monoester lipids when loaded into an SPE cartridge. Our suggested approach offers a valuable tool for developing efficient analytical procedures.

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  • 5.
    Hix Janssens, Thomas
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Shinde, Sudhirkumar
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Abouhany, Rahma
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Davies, Julia R
    Malmö University, Faculty of Odontology (OD). Malmö University, Biofilms Research Center for Biointerfaces.
    Neilands, Jessica
    Malmö University, Faculty of Odontology (OD). Malmö University, Biofilms Research Center for Biointerfaces.
    Svensäter, Gunnel
    Malmö University, Faculty of Odontology (OD). Malmö University, Biofilms Research Center for Biointerfaces.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Microcontact-Imprinted Optical Sensors for Virulence Factors of Periodontal Disease2023In: ACS Omega, E-ISSN 2470-1343, Vol. 8, no 17, p. 15259-15265Article in journal (Refereed)
    Abstract [en]

    Periodontitis (gum disease) is a common biofilm-mediated oral condition, with around 7% of the adult population suffering from severe disease with risk for tooth loss. Moreover, periodontitis virulence markers have been found in atherosclerotic plaque and brain tissue, suggesting a link to cardiovascular and Alzheimer’s diseases. The lack of accurate, fast, and sensitive clinical methods to identify patients at risk leads, on the one hand, to patients being undiagnosed until the onset of severe disease and, on the other hand, to overtreatment of individuals with mild disease, diverting resources from those patients most in need. The periodontitis-associated bacterium, Porphyromonas gingivalis, secrete gingipains which are highly active proteases recognized as key virulence factors during disease progression. This makes them interesting candidates as predictive biomarkers, but currently, there are no methods in clinical use for monitoring them. Quantifying the levels or proteolytic activity of gingipains in the periodontal pocket surrounding the teeth could enable early-stage disease diagnosis. Here, we report on a monitoring approach based on high-affinity microcontact imprinted polymer-based receptors for the Arg and Lys specific gingipains Rgp and Kgp and their combination with surface plasmon resonance (SPR)-based biosensor technology for quantifying gingipain levels in biofluids and patient samples. Therefore, Rgp and Kgp were immobilized on glass coverslips followed by microcontact imprinting of poly-acrylamide based films anchored to gold sensor chips. The monomers selected were N-isopropyl acrylamide (NIPAM), N-hydroxyethyl acrylamide (HEAA) and N-methacryloyl-4-aminobenzamidine hydrochloride (BAM), with N,N′-methylene bis(acrylamide) (BIS) as the crosslinker. This resulted in imprinted surfaces exhibiting selectivity towards their templates high affinity and selectivity for the templated proteins with dissociation constants (Kd) of 159 and 299 nM for the Rgp- and Kgp-imprinted, surfaces respectively. The former surface displayed even higher affinity (Kd = 71 nM) when tested in dilute cell culture supernatants. Calculated limits of detection for the sensors were 110 and 90 nM corresponding to levels below clinically relevant concentrations.

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  • 6.
    Huynh, Chau Minh
    et al.
    Department of Chemistry, Umeå University, S-901 87 Umeå, Sweden.
    Arribas Díez, Ignacio
    Department of Biochemistry & Molecular Biology and VILLUM Center for Bioanalytical Sciences, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark.
    Thi, Hien Kim Le
    Department of Chemistry, Umeå University, S-901 87 Umeå, Sweden.
    Jensen, Ole N
    Department of Biochemistry & Molecular Biology and VILLUM Center for Bioanalytical Sciences, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Irgum, Knut
    Department of Chemistry, Umeå University, S-901 87 Umeå, Sweden.
    Terminally Phosphorylated Triblock Polyethers Acting Both as Templates and Pore-Forming Agents for Surface Molecular Imprinting of Monoliths Targeting Phosphopeptides2023In: ACS Omega, E-ISSN 2470-1343, Vol. 8, no 9, p. 8791-8803Article in journal (Refereed)
    Abstract [en]

    The novel process reported here described the manufacture of monolithic molecularly imprinted polymers (MIPs) using a terminally functionalized block copolymer as the imprinting template and pore-forming agent. The MIPs were prepared through a step-growth polymerization process using a melamine-formaldehyde precondensate in a biphasic solvent system. Despite having a relatively low imprinting factor, the use of MIP monolith in liquid chromatography demonstrated the ability to selectively target desired analytes. An MIP capillary column was able to separate monophosphorylated peptides from a tryptic digest of bovine serum albumin. Multivariate data analysis and modeling of the phosphorylated and nonphosphorylated peptide retention times revealed that the number of phosphorylations was the strongest retention contributor for peptide retention on the monolithic MIP capillary column.

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  • 7.
    Kislenko, Evgeniia
    et al.
    Chemical and Optical Sensing Division, Bundesanstalt für Materialforschung und -prüfung (BAM), Richard-Willstätter-Str. 11, D-12489 Berlin, Germany.
    Incel, Anil
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Gawlitza, Kornelia
    Chemical and Optical Sensing Division, Bundesanstalt für Materialforschung und -prüfung (BAM), Richard-Willstätter-Str. 11, D-12489 Berlin, Germany.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Rurack, Knut
    Chemical and Optical Sensing Division, Bundesanstalt für Materialforschung und -prüfung (BAM), Richard-Willstätter-Str. 11, D-12489 Berlin, Germany.
    Towards molecularly imprinted polymers that respond to and capture phosphorylated tyrosine epitopes using fluorescent bis-urea and bis-imidazolium receptors.2023In: Journal of materials chemistry. B, ISSN 2050-750X, E-ISSN 2050-7518, Vol. 11, no 45, p. 10873-10882Article in journal (Refereed)
    Abstract [en]

    Early detection of cancer is essential for successful treatment and improvement in patient prognosis. Deregulation of post-translational modifications (PTMs) of proteins, especially phosphorylation, is present in many types of cancer. Therefore, the development of materials for the rapid sensing of low abundant phosphorylated peptides in biological samples can be of great therapeutic value. In this work, we have synthesised fluorescent molecularly imprinted polymers (fMIPs) for the detection of the phosphorylated tyrosine epitope of ZAP70, a cancer biomarker. The polymers were grafted as nanometer-thin shells from functionalised submicron-sized silica particles using a reversible addition-fragmentation chain-transfer (RAFT) polymerisation. Employing the combination of fluorescent urea and intrinsically cationic bis-imidazolium receptor cross-linkers, we have developed fluorescent sensory particles, showing an imprinting factor (IF) of 5.0. The imprinted polymer can successfully distinguish between phosphorylated and non-phosphorylated tripeptides, reaching lower micromolar sensitivity in organic solvents and specifically capture unprotected peptide complements in a neutral buffer. Additionally, we have shown the importance of assessing the influence of counterions present in the MIP system on the imprinting process and final material performance. The potential drawbacks of using epitopes with protective groups, which can co-imprint with targeted functionality, are also discussed.

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  • 8.
    Banan, Kamran
    et al.
    Shahid Beheshti Univ Med Sci, Sch Pharm, Dept Pharmaceut, Tehran, Iran..
    Ghorbani-Bidkorbeh, Fatemeh
    Shahid Beheshti Univ Med Sci, Sch Pharm, Dept Pharmaceut, Tehran, Iran..
    Afsharara, Hanif
    Shahid Beheshti Univ Med Sci, Sch Pharm, Dept Med Chem, Tehran, Iran..
    Hatamabadi, Dara
    Shahid Beheshti Univ Med Sci, Sch Pharm, Dept Med Chem, Tehran, Iran..
    Landi, Behnaz
    Shahid Beheshti Univ Med Sci, Sch Pharm, Dept Pharmaceut, Tehran, Iran..
    Kecili, Rustem
    Anadolu Univ, Yunus Emre Vocat Sch Hlth Serv, Dept Med Serv & Tech, Eskisehir, Turkey..
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Nano-sized magnetic core-shell and bulk molecularly imprinted polymers for selective extraction of amiodarone from human plasma2022In: Analytica Chimica Acta, ISSN 0003-2670, E-ISSN 1873-4324, Vol. 1198, article id 339548Article in journal (Refereed)
    Abstract [en]

    Bulk and magnetic core-shell Molecularly Imprinted Polymers (MMIPs) have been introduced and compared to extract and determine amiodarone from a complex matrix, i.e., plasma, due to the importance of Therapeutic Drug Monitoring (TDM). Polymer synthesis was confirmed by FTIR, AFM, TGA, DLS, VSM, TEM, and the adsorption studies such as capacity, isothermal models, selectivity, and regeneration were performed to evaluate and compare polymer efficiency in extraction and separation of amiodarone from sample solutions and human plasma. Both nano-sized and bulk polymers successfully extracted the target molecule at the low therapeutic ranges and the overdose concentrations (recoveries of 98.38%-102.70%). The maximum adsorption capacity of the MMIPs was 42.5 mu g/mg compared with 2.6 mu g/mg for bulk polymers. The imprinting factors of the polymers were 15.12 and 6.84 for MMIPs and bulk, respectively. MMIPs and bulk polymers presented 4.68 and 1.66 selectivity factors, respectively, towards amiodarone compared with lidocaine. LOD, LOQ and enrichment factor in human plasma were 0.09, 0.28 mu g mL(-1), and 10 respectively. Recoveries of therapeutic concentration from plasma were 91.38 and 97.33% for bulk and MMIPs, respectively. MMIPs as an adsorbent in amiodarone extraction from plasma offered reduced necessary sample amount, less adsorbent consumption, reduced pretreatment time, and reduced elution solvent waste while yielding higher extraction recovery and more specificity for the target compared with the bulk polymer. Bulk polymers have a more straightforward synthesis procedure due to fewer synthesis steps and fewer variables, and Molecularly Imprinted Polymer Solid-phase Extraction (MIP-SPE) has already been introduced commercially. MMIPs prevail on a small scale, and in the context of a simple extraction, separation, or concentration in large-scale bioanalysis, efforts towards optimization and development of MMIPs can unearth tremendous opportunities for green chemistry principles. 

  • 9.
    Shinde, Sudhirkumar
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces. Dr Vishwanath Karad MIT World Peace Univ, Sch Consciousness, Pune 411038, Maharashtra, India..
    Mansour, Mona
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces. Egyptian Petr Res Inst, Anal & Evaluat Dept, 1 Ahmed Zomor St, Cairo, Egypt..
    Mavliutova, Liliia
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Incel, Anil
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Wierzbicka, Celina
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Abdel-Shafy, Hussein, I
    Natl Res Ctr, Water Res & Pollut Control Dept, Cairo 11727, Egypt..
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Oxoanion Imprinting Combining Cationic and Urea Binding Groups: A Potent Glyphosate Adsorber2022In: ACS Omega, E-ISSN 2470-1343, Vol. 7, no 1Article in journal (Refereed)
    Abstract [en]

    The use of polymerizable hosts in anion imprinting has led to powerful receptors with high oxyanion affinity and specificity in both aqueous and non-aqueous environments. As demonstrated in previous reports, a carefully tuned combination of orthogonally interacting binding groups, for example, positively charged and neutral hydrogen bonding monomers, allows receptors to be constructed for use in either organic or aqueous environments, in spite of the polymer being prepared in non-competitive solvent systems. We here report on a detailed experimental design of phenylphosphonic and benzoic acid-imprinted polymer libraries prepared using either urea-or thiourea-based host monomers in the presence or absence of cationic comonomers for charge-assisted anion recognition. A comparison of hydrophobic and hydrophilic crosslinking monomers allowed optimum conditions to be identified for oxyanion binding in non-aqueous, fully aqueous, or high-salt media. This showed that recognition improved with the water content for thiourea-based molecularly imprinted polymers (MIPs) based on hydrophobic EGDMA with an opposite behavior shown by the polymers prepared using the more hydrophilic crosslinker PETA. While the affinity of thiourea-based MIPs increased with the water content, the opposite was observed for the oxourea counterparts. Binding to the latter could however be enhanced by raising the pH or by the introduction of cationic amine-or Na+-complexing crown ether-based comonomers. Use of high-salt media as expected suppressed the amine-based charge assistance, whereas it enhanced the effect of the crown ether function. Use of the optimized receptors for removing the ubiquitous pesticide glyphosate from urine finally demonstrated their practical utility.

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  • 10.
    Mahajan, Rashmi
    et al.
    Linnaeus Univ, Ctr Biomat Chem, Dept Chem & Biomed Sci, Bioorgan & Biophys Chem Lab, S-39182 Kalmar, Sweden..
    Suriyanarayanan, Subramanian
    Linnaeus Univ, Ctr Biomat Chem, Dept Chem & Biomed Sci, Bioorgan & Biophys Chem Lab, S-39182 Kalmar, Sweden..
    Olsson, Gustaf D.
    Linnaeus Univ, Ctr Biomat Chem, Dept Chem & Biomed Sci, Bioorgan & Biophys Chem Lab, S-39182 Kalmar, Sweden..
    Wiklander, Jesper G.
    Linnaeus Univ, Ctr Biomat Chem, Dept Chem & Biomed Sci, Bioorgan & Biophys Chem Lab, S-39182 Kalmar, Sweden..
    Aastrup, Teodor
    Attana AB, Greta Arwidssons Vag 21, S-11419 Stockholm, Sweden..
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Nicholls, Ian A.
    Linnaeus Univ, Ctr Biomat Chem, Dept Chem & Biomed Sci, Bioorgan & Biophys Chem Lab, S-39182 Kalmar, Sweden..
    Oxytocin-Selective Nanogel Antibody Mimics2022In: International Journal of Molecular Sciences, ISSN 1661-6596, E-ISSN 1422-0067, Vol. 23, no 5, article id 2534Article in journal (Refereed)
    Abstract [en]

    Oxytocin imprinted polymer nanoparticles were synthesized by glass bead supported solid phase synthesis, with NMR and molecular dynamics studies used to investigate monomer-template interactions. The nanoparticles were characterized by dynamic light scattering, scanning- and transmission electron microscopy and X-ray photoelectron spectroscopy. Investigation of nanoparticle-template recognition using quartz crystal microbalance-based studies revealed sub-nanomolar affinity, k(d) approximate to 0.3 +/- 0.02 nM (standard error of the mean), comparable to that of commercial polyclonal antibodies, k(d) approximate to 0.02-0.2 nM.

  • 11.
    Yeung, Sing Yee
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Sergeeva, Yulia
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Pan, Guoqing
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces. Institute for Advanced Materials, School of Materials Science and Engineering, Jiangsu University, Zhenjiang, Jiangsu 212 013, China.
    Mittler, Silvia
    Department of Physics and Astronomy, University of Western Ontario, 1151 Richmond Street, London, Ontario, Canada N6A 3K7.
    Ederth, Thomas
    Division of Biophysics and Bioengineering, Department of Physics, Chemistry and Biology (IFM), Linköping University, 581 83 Linköping, Sweden.
    Dam, Tommy
    Division of Physical Chemistry, Department of Chemistry, Lund University, 221 00 Lund, Sweden.
    Jönsson, Peter
    Division of Physical Chemistry, Department of Chemistry, Lund University, 221 00 Lund, Sweden.
    El-Schich, Zahra
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Gjörloff Wingren, Anette
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Tillo, Adam
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Hsiung Mattisson, Sabrina
    ImaGene-iT AB, Medicon Village, Scheelevägen 2, 223 81 Lund, Sweden.
    Holmqvist, Bo
    ImaGene-iT AB, Medicon Village, Scheelevägen 2, 223 81 Lund, Sweden.
    Stollenwerk, Maria M
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Reversible Self-Assembled Monolayers with Tunable Surface Dynamics for Controlling Cell Adhesion Behavior.2022In: ACS Applied Materials and Interfaces, ISSN 1944-8244, E-ISSN 1944-8252, Vol. 14, no 37, p. 41790-41799Article in journal (Refereed)
    Abstract [en]

    Cells adhering onto surfaces sense and respond to chemical and physical surface features. The control over cell adhesion behavior influences cell migration, proliferation, and differentiation, which are important considerations in biomaterial design for cell culture, tissue engineering, and regenerative medicine. Here, we report on a supramolecular-based approach to prepare reversible self-assembled monolayers (rSAMs) with tunable lateral mobility and dynamic control over surface composition to regulate cell adhesion behavior. These layers were prepared by incubating oxoacid-terminated thiol SAMs on gold in a pH 8 HEPES buffer solution containing different mole fractions of ω-(ethylene glycol)2-4- and ω-(GRGDS)-, α-benzamidino bolaamphiphiles. Cell shape and morphology were influenced by the strength of the interactions between the amidine-functionalized amphiphiles and the oxoacid of the underlying SAMs. Dynamic control over surface composition, achieved by the addition of inert filler amphiphiles to the RGD-functionalized rSAMs, reversed the cell adhesion process. In summary, rSAMs featuring mobile bioactive ligands offer unique capabilities to influence and control cell adhesion behavior, suggesting a broad use in biomaterial design, tissue engineering, and regenerative medicine.

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  • 12.
    Li, Qianjin
    et al.
    Nanjing Normal Univ, Sch Food Sci & Pharmaceut Engn, Nanjing 210023, Peoples R China..
    Wang, Tingting
    Nanjing Normal Univ, Sch Food Sci & Pharmaceut Engn, Nanjing 210023, Peoples R China..
    Jin, Yu
    Nanjing Normal Univ, Sch Food Sci & Pharmaceut Engn, Nanjing 210023, Peoples R China..
    Wierzbicka, Celina
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Wang, Fenying
    Nanchang Univ, Coll Chem, Nanchang 330031, Jiangxi, Peoples R China..
    Li, Jianlin
    Nanjing Normal Univ, Sch Food Sci & Pharmaceut Engn, Nanjing 210023, Peoples R China..
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Synthesis of highly selective molecularly imprinted nanoparticles by a solid-phase imprinting strategy for fluorescence turn-on recognition of phospholipid2022In: Sensors and actuators. B, Chemical, ISSN 0925-4005, E-ISSN 1873-3077, Vol. 368, article id 132193Article in journal (Refereed)
    Abstract [en]

    Molecularly imprinted polymers (MIPs) are artificial receptors with template tailored recognition sites complementary to the targets. The versatility of this molecular imprinting technique has been hampered by the lack of practical synthetic procedures to prepare highly selective MIP nanoparticles targeting phospholipids, which are challenging to be imprinted due to their amphiphilic structure. Here, a novel sedimentation-based solid phase imprinting strategy is introduced relying on polymerization in the presence of template-modified silica nanospheres (SNs). To demonstrate this concept, the sphingosine-1-phosphate receptor agonist fingolimod phosphate (FP) was coupled to SNs which were dispersed in the prepolymerization medium consisting of the fluorescent functional monomer 1,8-bis(N-vinylimidazol-N'-methyl)anthracene bromide and the crosslinking monomer ethyleneglycol dimethacrylate. High dilution polymerization of the dispersion under agitation followed by simple sedimentation-based separation of the SN template resulted in the isolation of surface imprinted fluorescent MIP nanoparticles (FMIP NPs) in a high yield (17 %). The FMIP NPs displayed fluorescence enhancement in response to the template with a high imprinting factor (IF=9) under the experimental conditions and good specificity, and could recognize FP in human serum with recoveries of 68-74 %. Moreover, the template-modified SNs could be recycled for reuse. Such molecular imprinting strategy opens a new approach to produce highly selective artificial receptors targeting phospholipids.

  • 13.
    Mavliutova, Liliia
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Verduci, Elena
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Combinatorial design of a sialic acid imprinted binding site exploring a dual ion receptor approach2021In: RSC Advances, E-ISSN 2046-2069, Vol. 11, no 54, article id 34329Article in journal (Refereed)
    Abstract [en]

    Aberrant sialic acid expression is one of the key indicators of pathological processes. This acidic saccharide is overexpressed in tumor cells and is a potent biomarker. Development of specific capture tools for various sialylated targets is an important step for early cancer diagnosis. However, sialic acid recognition by synthetic hosts is often complicated due to the competition for the anion binding by their counterions, such as Na+ and K+. Here we report on the design of a sialic acid receptor via simultaneous recognition of both the anion and cation of the target analyte. The polymeric receptor was produced using neutral (thio)urea and crown ether based monomers for simultaneous complexation of sialic acid's carboxylate group and its countercation. Thiourea and urea based functional monomers were tested both in solution by 1H NMR titration and in a polymer matrix system for their ability to complex the sodium salt of sialic acid alone and in the presence of crown ether. Combination of both orthogonally acting monomers resulted in higher affinities for the template in organic solvent media. The imprinted polymers displayed enhanced sialic acid recognition driven to a significant extent by the addition of the macrocyclic cation host. The effect of various counterions and solvent systems on the binding affinities is reported. Binding of K+, Na+ and NH4+ salts of sialic acid exceeded the uptake of bulky lipophilic salts. Polymers imprinted with sialic or glucuronic acids displayed a preference for their corresponding templates and showed a promising enrichment of sialylated peptides from the tryptic digest of glycoprotein bovine fetuin.

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  • 14.
    Mavliutova, Liliia
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Verduci, Elena
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Shinde, Sudhirkumar
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Combinatorial Design of a Sialic Acid-Imprinted Binding Site2021In: ACS Omega, E-ISSN 2470-1343, Vol. 6, no 18, p. 12229-12237Article in journal (Refereed)
    Abstract [en]

    Aberrant glycosylation has been proven to correlate with various diseases including cancer. An important alteration in cancer progression is an increased level of sialylation, making sialic acid one of the key constituents in tumor-specific glycans and an interesting biomarker for a diversity of cancer types. Developing molecularly imprinted polymers (MIPs) with high affinity toward sialic acids is an important task that can help in early cancer diagnosis. In this work, the glycospecific MIPs are produced using cooperative covalent/noncovalent imprinting. We report here on the fundamental investigation of this termolecular imprinting approach. This comprises studies of the relative contribution of orthogonally interacting functional monomers and their synergetic behavior and the choice of different counterions on the molecular recognition properties for the sialylated targets. Combining three functional monomers targeting different functionalities on the template led to enhanced imprinting factors (IFs) and selectivities. This apparent cooperative effect was supported by H-1 NMR and fluorescence titrations of monomers with templates or template analogs. Moreover, highlighting the role of the template counterion use of tetrabutylammonium (TBA) salt of sialic acid resulted in better imprinting than that of sodium salts supported by both in solution interaction studies and in MIP rebinding experiments. The glycospecific MIPs display high affinity for sialylated targets, with an overall low binding of other nontarget saccharides.

  • 15.
    Mavliutova, Liliia
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Munoz Aldeguer, Bruna
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Wiklander, Jesper
    Linnaeus University.
    Wierzbicka, Celina
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Huynh, Chau Minh
    Umeå University.
    Nicholls, Ian A.
    Linnaeus University.
    Irgum, Knut
    Umeå University.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Discrimination between sialic acid linkage modes using sialyllactose-imprinted polymers2021In: RSC Advances, E-ISSN 2046-2069, Vol. 11, no 36, p. 22409-22418Article in journal (Refereed)
    Abstract [en]

    Glycosylation plays an important role in various pathological processes such as cancer. One key alteration in the glycosylation pattern correlated with cancer progression is an increased level as well as changes in the type of sialylation. Developing molecularly-imprinted polymers (MIPs) with high affinity for sialic acid able to distinguish different glycoforms such as sialic acid linkages is an important task which can help in early cancer diagnosis. Sialyllactose with alpha 2,6 ' vs. alpha 2,3 ' sialic acid linkage served as a model trisaccharide template. Boronate chemistry was employed in combination with a library of imidazolium-based monomers targeting the carboxylate group of sialic acid. The influence of counterions of the cationic monomers and template on their interactions was investigated by means of H-1 NMR titration studies. The highest affinities were afforded using a combination of Br- and Na+ counterions of the monomers and template, respectively. The boronate ester formation was confirmed by MS and H-1/B-11 NMR, indicating 1 : 2 stoichiometries between sialyllactoses and boronic acid monomer. Polymers were synthesized in the form of microparticles using boronate and imidazolium monomers. This combinatorial approach afforded MIPs selective for the sialic acid linkages and compatible with an aqueous environment. The molecular recognition properties with respect to saccharide templates and glycosylated targets were reported.

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  • 16.
    Incel, Anıl
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Arribas Díez, Ignacio
    University of Southern Denmark, Odense.
    Wierzbicka, Celina
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Gajoch, Katarzyna
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Jensen, Ole N
    University of Southern Denmark, Odense.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Selective Enrichment of Histidine Phosphorylated Peptides Using Molecularly Imprinted Polymers2021In: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 93, no 8, p. 3857-3866Article in journal (Refereed)
    Abstract [en]

    Protein histidine phosphorylation (pHis) is involved in molecular signaling networks in bacteria, fungi, plants, and higher eukaryotes including mammals and is implicated in human diseases such as cancer. Detailed investigations of the pHis modification are hampered due to its acid-labile nature and consequent lack of tools to study this post-translational modification (PTM). We here demonstrate three molecularly imprinted polymer (MIP)-based reagents, MIP1-MIP3, for enrichment of pHis peptides and subsequent characterization by chromatography and mass spectrometry (LC-MS). The combination of MIP1 and β-elimination provided some selectivity for improved detection of pHis peptides. MIP2 was amenable to larger pHis peptides, although with poor selectivity. Microsphere-based MIP3 exhibited improved selectivity and was amenable to enrichment and detection by LC-MS of pHis peptides in tryptic digests of protein mixtures. These MIP protocols do not involve any acidic solvents during sample preparation and enrichment, thus preserving the pHis modification. The presented proof-of-concept results will lead to new protocols for highly selective enrichment of labile protein phosphorylations using molecularly imprinted materials.

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  • 17.
    El-Schich, Zahra
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Zhang, Yuecheng
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Göransson, Tommy
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Dizeyi, Nishtman
    Lund University.
    Persson, Jenny L.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces. Umeå University.
    Johansson, Emil
    Umeå University.
    Caraballo, Remi
    Umeå University.
    Elofsson, Mikael
    Umeå University.
    Shinde, Sudhirkumar
    World Peace University, India.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Gjörloff Wingren, Anette
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Sialic Acid as a Biomarker Studied in Breast Cancer Cell Lines In Vitro Using Fluorescent Molecularly Imprinted Polymers2021In: Applied Sciences, E-ISSN 2076-3417, Vol. 11, no 7, article id 3256Article in journal (Refereed)
    Abstract [en]

    Sialylations are post-translational modifications of proteins and lipids that play important roles in many cellular events, including cell-cell interactions, proliferation, and migration. Tumor cells express high levels of sialic acid (SA), which are often associated with the increased invasive potential in clinical tumors, correlating with poor prognosis. To overcome the lack of natural SA-receptors, such as antibodies and lectins with high enough specificity and sensitivity, we have used molecularly imprinted polymers (MIPs), or "plastic antibodies", as nanoprobes. Because high expression of epithelial cell adhesion molecule (EpCAM) in primary tumors is often associated with proliferation and a more aggressive phenotype, the expression of EpCAM and CD44 was initially analyzed. The SA-MIPs were used for the detection of SA on the cell surface of breast cancer cells. Lectins that specifically bind to the a-2,3 SA and a-2,6 SA variants were used for analysis of SA expression, with both flow cytometry and confocal microscopy. Here we show a correlation of EpCAM and SA expression when using the SA-MIPs for detection of SA. We also demonstrate the binding pattern of the SA-MIPs on the breast cancer cell lines using confocal microscopy. Pre-incubation of the SA-MIPs with SA-derivatives as inhibitors could reduce the binding of the SA-MIPs to the tumor cells, indicating the specificity of the SA-MIPs. In conclusion, the SA-MIPs may be a new powerful tool in the diagnostic analysis of breast cancer cells.

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  • 18.
    Ambaw, Y. A.
    et al.
    Precision Medicine Translational Research Programme and Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 119077, Singapore; SLING, Singapore Lipidomics Incubator, Life Sciences Institute, National University of Singapore, Singapore 119077, Singapore; Department of Molecular Metabolism, Harvard T.H. Chan School of Public Health, Harvard University, Cambridge, MA 02138, USA.
    Dahl, S. R.
    Department of Chemistry, University of Oslo, 0315 Oslo, Norway; Hormone Laboratory, Department of Medical Biochemistry, Oslo University Hospital, 0424 Oslo, Norway.
    Chen, Y.
    Department of Chemistry, University of Oslo, 0315 Oslo, Norway.
    Greibrokk, T.
    Department of Chemistry, University of Oslo, 0315 Oslo, Norway.
    Lundanes, E.
    Department of Chemistry, University of Oslo, 0315 Oslo, Norway.
    Lazraq, Issam
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Shinde, Sudhirkumar
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces. School of Consciousness, Dr Vishwanath Karad Maharashtra Institute of Technology–World Peace University, Kothrud, Pune 411038, Maharashtra, India.
    Selvalatchmanan, J.
    Precision Medicine Translational Research Programme and Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 119077, Singapore; SLING, Singapore Lipidomics Incubator, Life Sciences Institute, National University of Singapore, Singapore 119077, Singapore.
    Wenk, M. R.
    Precision Medicine Translational Research Programme and Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 119077, Singapore; SLING, Singapore Lipidomics Incubator, Life Sciences Institute, National University of Singapore, Singapore 119077, Singapore.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Torta, F.
    Precision Medicine Translational Research Programme and Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 119077, Singapore; SLING, Singapore Lipidomics Incubator, Life Sciences Institute, National University of Singapore, Singapore 119077, Singapore.
    Tailored polymer-based selective extraction of lipid mediators from biological samples2021In: Metabolites, ISSN 2218-1989, E-ISSN 2218-1989, Vol. 11, no 8, article id 539Article in journal (Refereed)
    Abstract [en]

    Lipid mediators, small molecules involved in regulating inflammation and its resolution, are a class of lipids of wide interest as their levels in blood and tissues may be used to monitor health and disease states or the effect of new treatments. These molecules are present at low levels in biological samples, and an enrichment step is often needed for their detection. We describe a rapid and selective method that uses new low-cost molecularly imprinted (MIP) and non-imprinted (NIP) polymeric sorbents for the extraction of lipid mediators from plasma and tissue samples. The extraction process was carried out in solid-phase extraction (SPE) cartridges, manually packed with the sorbents. After extraction, lipid mediators were quantified by liquid chromatography–tandem mass spectrometry (LC–MSMS). Various parameters affecting the extraction efficiency were evaluated to achieve optimal recovery and to reduce non-specific interactions. Preliminary tests showed that MIPs, designed using the prostaglandin biosynthetic precursor arachidonic acid, could effectively enrich prostaglandins and structurally related molecules. However, for other lipid mediators, MIP and NIP displayed comparable recoveries. Under optimized conditions, the recoveries of synthetic standards ranged from 62% to 100%. This new extraction method was applied to the determination of the lipid mediators concentration in human plasma and mouse tissues and compared to other methods based on commercially available cartridges. In general, the methods showed comparable performances. In terms of structural specificity, our newly synthesized materials accomplished better retention of prostaglandins (PGs), hydroxydocosahexaenoic acid (HDoHE), HEPE, hydroxyeicosatetraenoic acids (HETE), hydroxyeicosatrienoic acid (HETrE), and PUFA compounds, while the commercially available Strata-X showed a higher recovery for dihydroxyeicosatetraenoic acid (diHETrEs). In summary, our results suggest that this new material can be successfully implemented for the extraction of lipid mediators from biological samples. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

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  • 19.
    Shinde, Sudhirkumar
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Mansour, Mona
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Incel, Anil
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Mavliutova, Liliia
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Wierzbicka, Celina
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    High salt compatible oxyanion receptors by dual ion imprinting2020In: Chemical Science, ISSN 2041-6520, E-ISSN 2041-6539, Vol. 11, no 16, p. 4246-4250Article in journal (Refereed)
    Abstract [en]

    The design of hosts for either cations or anions is complicated due to the competition for binding by the host or guest counterions. Imprinting relying on self-assembly offers the possibility to stabilize the guest and its counterion in a favorable geometry. We here report on a comprehensive supramolecular approach to anion receptor design relying on concurrent recognition of both anion and cation. This was achieved by high order complex imprinting of the disodium salt of phenyl-phosphonic acid in combination with neutral urea and sodium ion selective 18-crown-6 monomers. The polymers displayed enhanced affinity for the template or inorganic phosphate or sulfate in competitive aqueous buffers, with affinity and selectivity increasing with increasing ionic strength. The presence of engineered sites for both ionic species dramatically increases the salt uptake in strongly competitive media such as brine.

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  • 20.
    Gornik, Tjasa
    et al.
    Department of Environmental Sciences, Jozef Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia; Jozef Stefan International Postgraduate School, Jamova 39, 1000 Ljubljana, Slovenia.
    Shinde, Sudhirkumar
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces. School of Chemistry and Chemical Engineering, Queens University Belfast, Belfast BT9 5AG, UK.
    Lamovsek, Lea
    Department of Biopharmacy and Pharmacokinetics, Faculty of Pharmacy, University of Ljubljana, Askerceva 7, 1000 Ljubljana, Slovenia.
    Koblar, Maja
    Jozef Stefan International Postgraduate School, Jamova 39, 1000 Ljubljana, Slovenia; Center for Electron Microscopy and Microanalysis (CEMM), Jamova 39, 1000 Ljubljana, Slovenia.
    Heath, Ester
    Department of Environmental Sciences, Jozef Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia; Jozef Stefan International Postgraduate School, Jamova 39, 1000 Ljubljana, Slovenia.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Kosjek, Tina
    Department of Environmental Sciences, Jozef Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia; Jozef Stefan International Postgraduate School, Jamova 39, 1000 Ljubljana, Slovenia.
    Molecularly Imprinted Polymers for the Removal of Antidepressants from Contaminated Wastewater.2020In: Polymers, E-ISSN 2073-4360, Vol. 13, no 1, article id E120Article in journal (Refereed)
    Abstract [en]

    Selective serotonin reuptake inhibitors (SSRIs) are a class of antidepressants regularly detected in the environment. This indicates that the existing wastewater treatment techniques are not successfully removing them beforehand. This study investigated the potential of molecularly imprinted polymers (MIPs) to serve as sorbents for removal of SSRIs in water treatment. Sertraline was chosen as the template for imprinting. We optimized the composition of MIPs in order to obtain materials with highest capacity, affinity, and selectivity for sertraline. We report the maximum capacity of MIP for sertraline in water at 72.6 mg g-1, and the maximum imprinting factor at 3.7. The MIPs were cross-reactive towards other SSRIs and the metabolite norsertraline. They showed a stable performance in wastewater-relevant pH range between 6 and 8, and were reusable after a short washing cycle. Despite having a smaller surface area between 27.4 and 193.8 m2·g-1, as compared to that of the activated carbon at 1400 m2·g-1, their sorption capabilities in wastewaters were generally superior. The MIPs with higher surface area and pore volume that formed more non-specific interactions with the targets considerably contributed to the overall removal efficiency, which made them better suited for use in wastewater treatment.

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  • 21.
    Li, Qianjin
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Department of Food Science and Engineering, School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Nanjing, 210023, China.
    Shinde, Sudhirkumar
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Grasso, Giuliana
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Caroli, Antonio
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Abouhany, Rahma
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Lanzillotta, Michele
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Pan, Guoqing
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Institute for Advanced Materials, School of Materials Science and Engineering, Jiangsu University, Zhenjiang, Jiangsu, 212013, China.
    Wan, Wei
    Chemical and Optical Sensing Division 1.9, Bundesanstalt für Materialforschung und -prüfung (BAM), Richard-Willstätter-Straße 11, 12489, Berlin, Germany.
    Rurack, Knut
    Chemical and Optical Sensing Division 1.9, Bundesanstalt für Materialforschung und -prüfung (BAM), Richard-Willstätter-Straße 11, 12489, Berlin, Germany.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Selective detection of phospholipids using molecularly imprinted fluorescent sensory core-shell particles2020In: Scientific Reports, E-ISSN 2045-2322, Vol. 10, no 1, article id 9924Article in journal (Refereed)
    Abstract [en]

    Sphingosine-1-phosphate (S1P) is a bioactive sphingo-lipid with a broad range of activities coupled to its role in G-protein coupled receptor signalling. Monitoring of both intra and extra cellular levels of this lipid is challenging due to its low abundance and lack of robust affinity assays or sensors. We here report on fluorescent sensory core-shell molecularly imprinted polymer (MIP) particles responsive to near physiologically relevant levels of S1P and the S1P receptor modulator fingolimod phosphate (FP) in spiked human serum samples. Imprinting was achieved using the tetrabutylammonium (TBA) salt of FP or phosphatidic acid (DPPA·Na) as templates in combination with a polymerizable nitrobenzoxadiazole (NBD)-urea monomer with the dual role of capturing the phospho-anion and signalling its presence. The monomers were grafted from ca 300 nm RAFT-modified silica core particles using ethyleneglycol dimethacrylate (EGDMA) as crosslinker resulting in 10-20 nm thick shells displaying selective fluorescence response to the targeted lipids S1P and DPPA in aqueous buffered media. Potential use of the sensory particles for monitoring S1P in serum was demonstrated on spiked serum samples, proving a linear range of 18-60 µM and a detection limit of 5.6 µM, a value in the same range as the plasma concentration of the biomarker.

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  • 22.
    Shinde, Sudhirkumar
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Faculty of Chemistry, Technical University of Dortmund, Otto-Hahn-Straße 6, 44227, Dortmund, Germany.
    Incel, Anil
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Mansour, Mona
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Olsson, Gustaf D
    Bioorganic & Biophysical Chemistry Laboratory, Linneaus University Center for Biomaterials Chemistry, Department of Chemistry & Biomedical Sciences, Linnaeus University, 39182 Kalmar, Sweden.
    Nicholls, Ian A
    Bioorganic & Biophysical Chemistry Laboratory, Linneaus University Center for Biomaterials Chemistry, Department of Chemistry & Biomedical Sciences, Linnaeus University, 39182 Kalmar, Sweden.
    Esen, Cem
    Faculty of Chemistry, Technical University of Dortmund, Otto-Hahn-Straße 6, 44227, Dortmund, Germany.
    Urraca, Javier
    Faculty of Chemistry, Technical University of Dortmund, Otto-Hahn-Straße 6, 44227, Dortmund, Germany.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces. Faculty of Chemistry, Technical University of Dortmund, Otto-Hahn-Straße 6, 44227, Dortmund, Germany.
    Urea-Based Imprinted Polymer Hosts with Switchable Anion Preference2020In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 142, no 26, p. 11404-11416Article in journal (Refereed)
    Abstract [en]

    The design of artificial oxyanion receptors with switchable ion preference is a challenging goal in host–guest chemistry. We here report on molecularly imprinted polymers (MIPs) with an external phospho-sulpho switch driven by small molecule modifiers. The polymers were prepared by hydrogen bond-mediated imprinting of the mono- or dianions of phenyl phosphonic acid (PPA), phenyl sulfonic acid (PSA), and benzoic acid (BA) using N-3,5-bis-(trifluoromethyl)-phenyl-Ń-4-vinylphenyl urea (1) as the functional host monomer. The interaction mode between the functional monomer and the monoanions was elucidated by 1H NMR titrations and 1H–1H NMR NOESY supported by molecular dynamic simulation, which confirmed the presence of high-order complexes. PPA imprinted polymers bound PPA with an equilibrium constant Keq = 1.8 × 105 M–1 in acetonitrile (0.1% 1,2,2,6,6-pentamethylpiperidine) and inorganic HPO42– and SO42– with Keq = 2.9 × 103 M–1 and 4.5 × 103 M–1, respectively, in aqueous buffer. Moreover, the chromatographic retentivity of phosphonate versus sulfonate was shown to be completely switched on this polymer when changing from a basic to an acidic modifier. Mechanistic insights into this system were obtained from kinetic investigations and DSC-, MALDI-TOF-MS-, 1H NMR-studies of linear polymers prepared in the presence of template. The results suggest the formation of template induced 1–1 diad repeats in the polymer main chain shedding unique light on the relative contributions of configurational and conformational imprinting.

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  • 23.
    Bergdahl, Gizem Ertürk
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). CapSenze Biosystems AB, Lund, Sweden.
    Akhoundian, Maedeh
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Lueg-Althoff, Kyra
    Department of Chemistry, University of Duisburg-Essen, Universitätsstr. 7, Essen, 45117, Germany.
    Shinde, Sudhirkumar
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces. School of Chemistry and Chemical Engineering, Queens University Belfast, Northern Ireland, United Kingdom.
    Yeung, Sing Yee
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Hedström, Martin
    CapSenze Biosystems AB, Lund, 223 63, Sweden; Department of Biotechnology, Lund University, Lund, 223 62, Sweden.
    Schrader, Thomas
    Department of Chemistry, University of Duisburg-Essen, Universitätsstr. 7, Essen, 45117, Germany.
    Mattiasson, Bo
    CapSenze Biosystems AB, Lund, 223 63, Sweden; Department of Biotechnology, Lund University, Lund, 223 62, Sweden.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Bisphosphonate Ligand Mediated Ultrasensitive Capacitive Protein Sensor: Complementary Match of Supramolecular and Dynamic Chemistry2019In: New Journal of Chemistry, ISSN 1144-0546, E-ISSN 1369-9261, Vol. 43, no 2, p. 847-852Article in journal (Refereed)
    Abstract [en]

    Modern healthcare demands rapid and accurate detection of proteins/enzymes at the ultratrace level. Herein we present a molecularly imprinted capacitive sensor for Trypsin, developed by microcontact imprinting. High affinity and selectivity was achieved by doping the prepolymerization mixture with a stoichiometric amount of methacrylamide-based bisphosphonate (BP) monomer. Taking advantage of the strong interaction of bisphosphonate with lysine/arginine residues on the surface of Trypsin, we have constructed a powerful polymeric sensor. The BP based sensor has the ability to recognize trypsin over other arginine-rich proteins, even in high ionic strength buffers with a sub-picomolar detection limit (pM). We believe that the combination of supramolecular chemistry, molecular imprinting and advanced instrumentation has a potential for future drug development and diagnostics that extends beyond biomolecular recognition.

  • 24.
    Zhang, Yuecheng
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Llapashtica, Kushtrim
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Shinde, Sudhirkumar
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    El-Schich, Zahra
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Gjörloff Wingren, Anette
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Determination of cytokine regulated glycan expression by using molecularly imprinted polymers targeting sialic acid2019In: Journal of cancer metastasis and treatment, ISSN 2454-2857, Vol. 56, no 5Article in journal (Refereed)
    Abstract [en]

    Cancer cells often have an increased amount of glycans, such as sialic acid (SA), on the cell surface, which normally play an important role in cell growth, proliferation and differentiation. In this study, SA expression is determined by fluorescent nanoprobes, molecularly imprinted polymers, SA-MIPs. The nanoprobes are synthesized with an imprinting approach to produce tailor-made fluorescent core-shell particles with high affinity for cell surface SA. Inflammation and cytokine production are well known tumor promoters, modulating the cellular microenvironment, including an aberrant cell surface glycan pattern. The recombinant cytokines IL-4, IL-6, IL-8 and a cocktail of cytokines collected from stimulated T leukemia Jurkat cells were used to induce in vitro inflammation in two cell lines, and thereafter analyzed with the use of SA-MIPs and flow cytometry. One of cell lines showed a different binding pattern of SA-MIPs after treatment with recombinant cytokines and the cytokine cocktail. This study shows that SA-MIPs can be an important tool in the investigation of overexpressed glycans in the tumor microenvironment.

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  • 25.
    Moczko, Ewa
    et al.
    Departamento de Química Ambiental, Facultad de Ciencias, Universidad Católica de la Santísima Concepción, Chile.
    Guerreiro, Antonio
    MIP Diagnostics Ltd., Fielding Johnson Building, University of Leicester, Leicester, UK.
    Caceres, Cesar
    Departamento de Polímeros, Facultad de Ciencias Químicas, Universidad de Concepción, Chile.
    Piletska, Elena
    Department of Chemistry, University of Leicester, Leicester, UK.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Piletsky, Sergey A.
    Department of Chemistry, University of Leicester, Leicester, UK.
    Epitope approach in molecular imprinting of antibodies2019In: Journal of chromatography. B, ISSN 1570-0232, E-ISSN 1873-376X, Vol. 1124, p. 1-6Article in journal (Refereed)
    Abstract [en]

    Herein an approach to prepare molecularly imprinted polymer nanoparticles (nanoMlPs) with specific binding affinity for antibodies is reported. The process relied on the covalent immobilization of the template (whole immunoglobulin G (IgG), Fc domain of human IgG and peptide epitope) onto the surface of a solid support, polymerization and affinity separation of nanoMlPs. The binding between nanoMIPs and their corresponding templates was analyzed and evaluated as being in sub-nanomolar and nano-molar range. The nanoMlPs prepared for Fc domain and epitope demonstrated a specific recognition of both human and goat IgGs, therefore they could be considered as a synthetic analogue of protein A and benefit from its intrinsic stability, short time and low cost of preparation.

  • 26.
    Olsson, Annsofie (Curator, Creator)
    Malmö University, Malmö University Library.
    Dorthé, Lotti (Curator)
    Malmö University, Malmö University Library.
    Tosting, Åsa (Designer)
    Malmö University, Malmö University Library.
    Brandström, Maria (Designer)
    Malmö University, Malmö University Library.
    Svensson, Anneli (Contributor)
    Malmö University, Malmö University Library.
    Wingren Gjörloff, Anette (Researcher)
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Sellergren, Börje (Researcher)
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Mavliutova, Liliia (Researcher)
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Zhang, Yuecheng (Researcher)
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Sternbæk, Louise (Researcher)
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Karlsson, Richard (Researcher)
    Københavns Universitet.
    Forskarnas Galleri #7: Fighting cancer with plastic bullets2019Artistic output (Unrefereed)
    Abstract [en]

    Cancer is a term used for about 200 different diseases. What they all have in common is that the cells in the body start to divide uncontrollably. In 2018 there were 18 million cancer cases around the world. In Sweden, approximately every third person will be diagnosed with a cancer disease at some point during their lifetime.A major challenge for science is to find ways to diagnose and treat these diseases. At Malmö university a new generation of chemists, physicists and biologists work in two international networks, BioCapture and GlycoImaging. Their research focus on designing plastic antibodies, bullets. The bullets are cheap to produce and aim to detect cancer cells at an early stage.

    The two projects are coordinated by Börje Sellergren and Anette Gjörloff Wingren, who train and tutor 19 PhD students. This exhibition highlights the interdisciplinary work of the PhD’s and their importance for the cancer research.

  • 27.
    Mahajan, Rashmi
    et al.
    Bioorganic and Biophysical Chemistry Laboratory, Linnaeus University Centre for Biomaterials Chemistry, Department of Chemistry and Biomedical Sciences, Linnaeus University, 391 82, Kalmar, Sweden.
    Rouhi, Mona
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Shinde, Sudhirkumar
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Bedwell, Thomas
    Chemistry Department, College of Science and Engineering, University of Leicester, Leicester, LE1 7RH, UK.
    Incel, Anil
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Mavliutova, Liliia
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Piletsky, Sergey
    Chemistry Department, College of Science and Engineering, University of Leicester, Leicester, LE1 7RH, UK.
    Nicholls, Ian
    Bioorganic and Biophysical Chemistry Laboratory, Linnaeus University Centre for Biomaterials Chemistry, Department of Chemistry and Biomedical Sciences, Linnaeus University, 391 82, Kalmar, Sweden.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Highly efficient synthesis and assay of protein imprinted nanogels using magnetic templates2019In: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 58, no 3Article in journal (Refereed)
    Abstract [en]

    We here report an approach integrating synthesis and a highly sensitive as-say of protein imprinted nanogels ("plastic antibodies") employing templates attached to magnetic carriers. The proteolytic enzymes trypsin and pepsin were immobilized on aminofunctionalized solgel coated magnetic nanoparticles (magNPs). Lightly crosslinked fluorescently doped polyacrylamide nanogels were subsequently produced by high dilution polymerization of monomers in presence of 50 mg of the magNPs. This was followed by multiple washes of the magnetically trapped particles and collection of each fraction. Finally, a wash of the particles at elevated temperature led to elution of ca 10 mg of fluorescent nanogel taken on to further characterisation. This corresponded to a gravimetric yield of nanogel of ca 12% based on added monomer. The nanogels were characterised by a novel competitive fluorescence assay employing the identical protein conjugated nanoparticles as ligands to reversibly immobilize the corresponding nanogels. Both nanogels exhibited Kd < 10 pM for their respective target protein and low crossreactivity for five reference proteins. This agrees with affinities reported for solid phase synthesized nanogels prepared using low surface area glass bead supports. The integrated approach simplifies in a major way the development and produc-tion of plastic antibodies and offers direct access to a practical bioassay.

  • 28.
    Yeung, Sing Yee
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Sergeeva, Yulia
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Dam, Tommy
    Division of Physical Chemistry , Lund University , Box 124, 22100 Lund , Sweden.
    Jönsson, Peter
    Division of Physical Chemistry , Lund University , Box 124, 22100 Lund , Sweden.
    Pan, Guoqing
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Chaturvedi, Vivek
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Lipid Bilayer-like Mixed Self-Assembled Monolayers with Strong Mobility and Clustering-Dependent Lectin Affinity2019In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 35, no 24, p. 8174-8181Article in journal (Refereed)
    Abstract [en]

    Glycans at the surface of cellular membranes modulate biological activity via multivalent association with extracellular messengers. The lack of tuneable simplified models mimicking this dynamic environment complicates basic studies of these phenomena. We here present a series of mixed reversible self-assembled monolayers (rSAMs) that addresses this deficiency. Mixed rSAMs were prepared in water by simple immersion of a negatively charged surface in a mixture of sialic acid- and hydroxy-terminated benzamidine amphiphiles. Surface compositions derived from infrared reflection-absorption spectroscopy (IRAS) and film thickness information (atomic force microscopy, ellipsometry) suggest the latter to be statistically incorporated in the monolayer. These surfaces' affinity for the lectin hemagglutinin revealed a strong dependence of the affinity on the presentation, density, and mobility of the sialic acid ligands. Hence, a spacer length of 4 ethylene glycol and a surface density of 15% resulted in a dissociation constant K-d,K-multi of 1.3 x 10(-13) M, on par with the best di- or tri-saccharide-based binders reported to date, whereas a density of 20% demonstrated complete resistance to hemagglutinin binding. These results correlated with ligand mobility measured by fluorescence recovery after photobleaching which showed a dramatic drop in the same interval. The results have a direct bearing on biological cell surface multivalent recognition involving lipid bilayers and may guide the design of model surfaces and sensors for both fundamental and applied studies.

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  • 29.
    Wang, Jixiang
    et al.
    Institute of Green Chemistry and Chemical Technology, School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang, Jiangsu, 212013, China; School of the Environment and Safety Engineering, Jiangsu University, Jiangsu, 212013, China.
    Dai, Jiangdong
    Institute of Green Chemistry and Chemical Technology, School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang, Jiangsu, 212013, China.
    Xu, Yeqing
    Institute of Green Chemistry and Chemical Technology, School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang, Jiangsu, 212013, China; School of the Environment and Safety Engineering, Jiangsu University, Jiangsu, 212013, China.
    Dai, Xiaohui
    Institute of Green Chemistry and Chemical Technology, School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang, Jiangsu, 212013, China.
    Zhang, Yunlei
    Institute of Green Chemistry and Chemical Technology, School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang, Jiangsu, 212013, China.
    Shi, Weidong
    Institute of Green Chemistry and Chemical Technology, School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang, Jiangsu, 212013, China.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Pan, Guoqing
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Institute for Advanced Materials, School of Materials Science and Engineering, Jiangsu University, Zhenjiang, Jiangsu, 212013, China.
    Molecularly Imprinted Fluorescent Test Strip for Direct, Rapid, and Visual Dopamine Detection in Tiny Amount of Biofluid2019In: Small, ISSN 1613-6810, E-ISSN 1613-6829, Vol. 15, no 1, article id e1803913Article in journal (Refereed)
    Abstract [en]

    Paper-based assays for detection of physiologically important species are needed in medical theranostics owning to their superiorities in point of care testing, daily monitoring, and even visual readout by using chromogenic materials. In this work, a facile test strip is developed for visual detection of a neurotransmitter dopamine (DA) based on dual-emission fluorescent molecularly imprinted polymer nanoparticles (DE-MIPs). The DE-MIPs, featured with tailor-made DA affinity and good anti-interference, exhibit DA concentration-dependent fluorescent colors, due to the variable ratios of dual-emission fluorescence caused by DA binding and quenching. By facile coating DE-MIPs on a filter paper, the DA test strips are obtained. The resultant test strip, like the simplicity of a pH test paper, shows the potential for directly visual detection of DA levels just by dripping a tiny amount of biofluid sample on it. The test result of real serum samples demonstrates that the DA strip enables to visually and semiquantitatively detect DA within 3 min by using only 10 microL of serum samples and with a low detection limit ((100-150) x 10(-9) m) by naked eye. This work thus offers a facile and efficient strategy for rapid, visual, and on-site detection of biofluids in clinic.

  • 30.
    Liu, Mingquan
    et al.
    Umeå University , Department of Chemistry , S-901 87 Umeå , Sweden.
    Torsetnes, Silje Bøen
    University of Southern Denmark , Department of Biochemistry and Molecular Biology and VILLUM Center for Bioanalytical Sciences , Campusvej 55 , DK-5230 Odense M , Denmark.
    Wierzbicka, Celina
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Jensen, Ole Nørregaard
    University of Southern Denmark , Department of Biochemistry and Molecular Biology and VILLUM Center for Bioanalytical Sciences , Campusvej 55 , DK-5230 Odense M , Denmark.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Irgum, Knut
    Umeå University , Department of Chemistry , S-901 87 Umeå , Sweden.
    Selective Enrichment of Phosphorylated Peptides by Monolithic Polymers Surface Imprinted with bis-Imidazolium Moieties by UV-Initiated Cryopolymerization2019In: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 91, no 15, p. 10188-10196Article in journal (Refereed)
    Abstract [en]

    Reversible protein phosphorylation on serine, threonine, and tyrosine residues is essential for fast, specific, and accurate signal transduction in cells. Up to now, the identification and quantification of phosphorylated amino acids, peptides, and proteins continue to be one of the significant challenges in contemporary bioanalytical research. In this paper, a series of surface grafted monoliths in the capillary format targeting phosphorylated serine has been prepared by first synthesizing a monolithic core substrate material based on trimethylolpropane trimethacrylate, onto which a thin surface-imprinted layer was established by oriented photografting of a variety of mono- and bis-imidazolium host monomers at subzero temperature, using six different continuous or pulsed UV light sources. The imprinted monolith capillaries were evaluated in a capillary liquid chromatographic system connected to a mass spectrometer in order to test the specific retention of phosphorylated peptides. Site-specific recognition selectivity and specificity for phosphorylated serine was demonstrated when separating amino acids and peptides, proving that the optimized materials could be used as novel trapping media in affinity-based phosphoproteomic analysis.

  • 31.
    Bakkour, Rani
    et al.
    Eawag , Swiss Federal Institute of Aquatic Science and Technology , CH-8600 Dübendorf , Switzerland; Institute of Biogeochemistry and Pollutant Dynamics , ETH Zürich , CH-8092 Zürich , Switzerland.
    Bolotin, Jakov
    Eawag , Swiss Federal Institute of Aquatic Science and Technology , CH-8600 Dübendorf , Switzerland.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Hofstetter, Thomas B.
    Eawag , Swiss Federal Institute of Aquatic Science and Technology , CH-8600 Dübendorf , Switzerland; Institute of Biogeochemistry and Pollutant Dynamics , ETH Zürich , CH-8092 Zürich , Switzerland.
    Molecularly Imprinted Polymers for Compound-Specific Isotope Analysis of Polar Organic Micropollutants in Aquatic Environments2018In: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 90, no 12, p. 7292-7301Article in journal (Refereed)
    Abstract [en]

    Compound-specific isotope analysis (CSIA) of polar organic micropollutants in environmental waters requires a processing of large sample volumes to obtain the required analyte masses for analysis by gas chromatography/isotoperatio mass spectrometry (GC/IRMS). However, the accumulation of organic matter of unknown isotopic composition in standard enrichment procedures currently compromises the accurate determination of isotope ratios. We explored the use of molecularly imprinted polymers (MIPs) for selective analyte enrichment for C-13/C-12 and N-15/N-14 ratio measurements by GC/IRMS using 1H-benzotriazole, a typical corrosion inhibitor in dishwashing detergents, as example of a widely detected polar organic micropollutant. We developed procedures for the treatment of >10 L of water samples, in which custom-made MIPs enabled the selective cleanup of enriched analytes in organic solvents obtained through conventional solid-phase extractions. Hydrogen bonding interactions between the triazole moiety of 1H-benzotriazole, and the MIP were responsible for selective interactions through an assessment of interaction enthalpies and N-15 isotope effects. The procedure was applied successfully without causing isotope fractionation to river water samples, as well as in- and effluents of wastewater treatment plants containing mu g/L concentrations of 1H-benzotriazole and dissolved organic carbon (DOC) loads of up to 28 mg C/L. MIP-based treatments offer new perspectives for CSIA of organic micropollutants through the reduction of the DOC-to-micropollutant ratios.

  • 32.
    Yeung, Sing Yee
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Ederth, Thomas
    Division of Molecular Physics, Department of Physics, Chemistry and Biology (IFM) , Linköping University , 581 83 Linköping , Sweden.
    Pan, Guoqing
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Cicenaite, Judita
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Cárdenas, Marité
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Arnebrant, Thomas
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Sellergren, Börje
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Reversible Self-Assembled Monolayers (rSAMs) as Robust and Fluidic Lipid Bilayer Mimics2018In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 34, no 13, p. 4107-4115Article in journal (Refereed)
    Abstract [en]

    Lipid bilayers, forming the outer barrier of cells, display a wide array of proteins and carbohydrates for modulating interfacial biological interactions. Formed by the spontaneous self-assembly of lipid molecules, these bilayers feature liquid crystalline order, while retaining a high degree of lateral mobility. Studies of these dynamic phenomena have been hampered by the fragility and instability of corresponding biomimetic cell membrane models. Here, we present the construct of a series of oligoethylene glycol-terminated reversible self-assembled monolayers (rSAMs) featuring lipid-bilayer-like fluidity, while retaining air and protein stability and resistance. These robust and ordered layers were prepared by simply immersing a carboxylic acid terminated self-assembled monolayer into 5-50 mu M aqueous omega-(4-ethylene glycol-phenoxy)-alpha-(4-amidinophenoxy)decane solutions. It is anticipated that this new class of robust and fluidic two-dimensional biomimetic surfaces will impact the design of rugged cell surface mimics and high-performance biosensors.

  • 33.
    Pan, Guoqing
    et al.
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces. Institute for Advanced Materials, School of Materials Science and Engineering, Jiangsu University, Zhenjiang, Jiangsu, 212013, China.
    Shinde, Sudhirkumar
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Yeung, Sing Yee
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Jagstaite, Migle
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Li, Qianjin
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Gjörloff Wingren, Anette
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    An Epitope Imprinted Biointerface with Dynamic Bioactivity for Modulating Cell-Biomaterial Interactions2017In: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 56, no 50, p. 15959-15963Article in journal (Refereed)
    Abstract [en]

    In this study, an epitope-imprinting strategy was employed for the dynamic display of bioactive ligands on a material interface. An imprinted surface was initially designed to exhibit specific affinity towards a short peptide (i.e., the epitope). This surface was subsequently used to anchor an epitope-tagged cell-adhesive peptide ligand (RGD: Arg-Gly-Asp). Owing to reversible epitope-binding affinity, ligand presentation and thereby cell adhesion could be controlled. As compared to current strategies for the fabrication of dynamic biointerfaces, for example, through reversible covalent or host–guest interactions, such a molecularly tunable dynamic system based on a surface-imprinting process may unlock new applications in in situ cell biology, diagnostics, and regenerative medicine.

  • 34.
    Rossetti, Cecilia
    et al.
    Department of Pharmaceutical Chemistry, University of Oslo, School of Pharmacy, Postbox 1068 Blindern, 0316 Oslo, Norway.
    Switnicka-Plak, Magdalena A.
    WestCHEM, Department of Pure and Applied Chemistry, University of Strathclyde, Thomas Graham Building, 295 Cathedral Street, Glasgow, G1 1XL, United Kingdom.
    Halvorsen, Trine Gronhaug
    Department of Pharmaceutical Chemistry, University of Oslo, School of Pharmacy, Postbox 1068 Blindern, 0316 Oslo, Norway.
    Cormack, Peter A. G.
    WestCHEM, Department of Pure and Applied Chemistry, University of Strathclyde, Thomas Graham Building, 295 Cathedral Street, Glasgow, G1 1XL, United Kingdom.
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Reubsaet, Leon
    Department of Pharmaceutical Chemistry, University of Oslo, School of Pharmacy, Postbox 1068 Blindern, 0316 Oslo, Norway.
    Automated Protein Biomarker Analysis: on-line extraction of clinical samples by Molecularly Imprinted Polymers2017In: Scientific Reports, E-ISSN 2045-2322, Vol. 7Article in journal (Refereed)
    Abstract [en]

    Robust biomarker quantification is essential for the accurate diagnosis of diseases and is of great value in cancer management. In this paper, an innovative diagnostic platform is presented which provides automated molecularly imprinted solid-phase extraction (MISPE) followed by liquid chromatography-mass spectrometry (LC-MS) for biomarker determination using ProGastrin Releasing Peptide (ProGRP), a highly sensitive biomarker for Small Cell Lung Cancer, as a model. Molecularly imprinted polymer microspheres were synthesized by precipitation polymerization and analytical optimization of the most promising material led to the development of an automated quantification method for ProGRP. The method enabled analysis of patient serum samples with elevated ProGRP levels. Particularly low sample volumes were permitted using the automated extraction within a method which was time-efficient, thereby demonstrating the potential of such a strategy in a clinical setting.

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  • 35.
    Wierzbicka, Celina
    et al.
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Liu, Mingquan
    Department of Chemistry, Umeå University, Umeå, 901 87, Sweden.
    Bauer, David
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Irgum, Knut
    Department of Chemistry, Umeå University, Umeå, 901 87, Sweden.
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Cationic pTyr/pSer imprinted polymers based on a bis-imidazolium host monomer: phosphopeptide recognition in aqueous buffers demonstrated by mu-liquid chromatography and monolithic columns2017In: Journal of materials chemistry. B, ISSN 2050-750X, E-ISSN 2050-7518, Vol. 5, no 5, p. 953-960Article in journal (Refereed)
    Abstract [en]

    We report on the design and characterization of imprinted cationic host polymers for selective trapping of phosphoserine and phosphotyrosine peptides. A series of imidazolium host monomers were synthesized and characterized with respect to binding affinity and stoichiometry of interaction with salts of phenylphosphonic acid. The strongest binders were subsequently used for the preparation of imprinted polymers in the form of crushed monoliths, using Fmoc-phosphotyrosine-ethyl ester or Fmoc-phosphoserine-ethyl ester as templates in combination with a hydrophilic crosslinking monomer. The polymers were compared with respect to binding and its dependence on solvent, and whether charged or uncharged host monomers were used. The recipes were subsequently implemented in the capillary monolith format for evaluation by micro-liquid chromatography in both buffered and organic media. Results from both tested formats reveal that the cationic host polymers displayed enhanced recognition in polar and buffered media, in contrast to neutral urea-based hosts which showed best results in acetonitrile rich mobile phases.

  • 36.
    Bakkour, Rani
    et al.
    Swiss Fed Inst Technol, Inst Biogeochem & Pollutant Dynam, Zurich, Switzerland; Eawag, Environm Chem, Dubendorf, Switzerland.
    Shinde, Sudhirkumar
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Hofstetter, Thomas
    Swiss Fed Inst Technol, Inst Biogeochem & Pollutant Dynam, Zurich, Switzerland; Eawag, Environm Chem, Dubendorf, Switzerland.
    Determination of source and fate of glyphosate in aqueous environments using molecularly-imprinted polymers and compound-specific isotope analysis2017In: Abstracts of Papers of the American Chemical Society, ISSN 0065-7727, Vol. 253Article in journal (Other academic)
  • 37.
    Rossetti, Cecilia
    et al.
    Department of Pharmaceutical Chemistry, School of Pharmacy, University of Oslo, P.O. Box 1068, Blindern, 0316, Oslo, Norway.
    Ore, Odd Gøran
    Department of Pharmaceutical Chemistry, School of Pharmacy, University of Oslo, P.O. Box 1068, Blindern, 0316, Oslo, Norway.
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Halvorsen, Trine Grønhaug
    Department of Pharmaceutical Chemistry, School of Pharmacy, University of Oslo, P.O. Box 1068, Blindern, 0316, Oslo, Norway.
    Reubsaet, Léon
    Department of Pharmaceutical Chemistry, School of Pharmacy, University of Oslo, P.O. Box 1068, Blindern, 0316, Oslo, Norway.
    Exploring the peptide retention mechanism in molecularly imprinted polymers2017In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 409, no 24, p. 5631-5643Article in journal (Refereed)
    Abstract [en]

    Molecularly imprinted polymers (MIPs) have been used as useful sorbents in solid-phase extraction for a wide range of molecules and sample matrices. Their unique selectivity can be fine-tuned in the imprinting process and is crucial for the extraction of macromolecules from complex matrices such as serum. A relevant example of this is the application of MIPs to peptides in diagnostic assays. In this article the selectivity of MIPs, previously implemented in a quantitative mass-spectrometric assay for the biomarker pro-gastrin-releasing peptide, is investigated. Partial least squares regression was used to generate models for the evaluation and prediction of the retention mechanism of MIPs. A hypothesis on interactions of MIPs with the target peptide was verified by ad hoc experiments considering the relevant peptide physicochemical properties highlighted from the multivariate analysis. Novel insights into and knowledge of the driving forces responsible for the MIP selectivity have been obtained and can be directly used for further optimization of MIP imprinting strategies. Graphical Abstract Applied analytical strategy: the Solid Phase Extraction (SPE) of digested Bovin Serum Albumin (BSA), using Molecularly Imprinted Polymers (MIP), is followed by the liquid chromatography-mass spectrometry (LC-MS) analysis for the identification of the retained peptides. The further application of multivariate analysis allows setting up a Partial Least Square (PLS) model, which describes the peptide retention into the MIP and gives additional knowledge to be used in the optimization of the MIP and the whole SPE method.

  • 38.
    Jagdadeesan, Kishore
    et al.
    Department of Biomedical Engineering, Lund University, Lund, Sweden.
    Rossetti, Cecilia
    Department of Pharmaceutical Chemistry, School of Pharmacy, University of Oslo, Oslo, Norway.
    Qader, Abed Abdel
    Department of Environmental Chemistry and Analytical Chemistry, Institute for Environmental Research (INFU), Technical University of Dortmund, Dortmund, Germany.
    Reubsaet, Leon
    Department of Pharmaceutical Chemistry, School of Pharmacy, University of Oslo, Oslo, Norway.
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Laurell, Thomas
    Department of Biomedical Engineering, Lund University, Lund, Sweden.
    Ekström, Simon
    Department of Biomedical Engineering, Lund University, Lund, Sweden.
    Filter Plate–Based Screening of MIP SPE Materials for Capture of the Biomarker Pro-Gastrin-Releasing Peptide2017In: SLAS Discovery, ISSN 2472-5552, Vol. 22, no 10, p. 1253-1261Article in journal (Refereed)
    Abstract [en]

    Affinity-based solid-phase extraction (SPE) is an attractive low-cost sample preparation strategy for biomarker analysis. Molecularly imprinted polymers (MIPs) as affinity sorbents offer unique opportunities for affinity SPE, due to their low manufacturing cost and high robustness. A limitation is the prediction of their affinity; therefore, screening of analyte recovery and specificity within a large range of SPE conditions is important in order to ensure high-sensitivity detection and assay reproducibility. Here, a µ-SPE method for screening of the MIP-SPE materials using a commercial 384-well filter plate is presented. The method allows for rapid and automated screening using 10?30 µL of packed SPE sorbent per well and sample volumes in the range of 10?70 µL. This enables screening of many different SPE sorbents while simultaneously identifying optimal SPE conditions. In addition, the 384-well format also facilitates detection with a multitude of analytical platforms. Performance of the µ-MIP-SP

  • 39.
    Wierzbicka, Celina
    et al.
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Torsetnes, Silje B.
    Department of Biochemistry and Molecular Biology, VILLUM Center for Bioanalytical Sciences, University of Southern Denmark, Odense M, DK-5230, Denmark.
    Jensen, Ole N.
    Department of Biochemistry and Molecular Biology, VILLUM Center for Bioanalytical Sciences, University of Southern Denmark, Odense M, DK-5230, Denmark.
    Shinde, Sudhirkumar
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Hierarchically templated beads with tailored pore structure for phosphopeptide capture and phosphoproteomics2017In: RSC Advances, E-ISSN 2046-2069, Vol. 7, no 28, p. 17154-17163Article in journal (Refereed)
    Abstract [en]

    Two templating approaches to produce imprinted phosphotyrosine capture beads with a controllable pore structure are reported and compared with respect to their ability to enrich phosphopeptides from a tryptic peptide mixture. The beads were prepared by the polymerization of urea-based host monomers and crosslinkers inside the pores of macroporous silica beads with both free and immobilized template. In the final step the silica was removed by fluoride etching resulting in mesoporous polymer replicas with narrow pore size distributions, pore diameters approximate to 10 nm and surface area > 260 m(2) g(-1). The beads displayed pronounced phosphotyrosine affinity and selectivity in binding tests using model peptides in acetonitrile rich solutions with a performance surpassing solution polymerized bulk imprinted materials. Tests of the beads for the enrichment of phosphopeptides from tryptic digests of twelve proteins revealed both pY/pS and pY/Y selectivity. This was reflected in a nearly 6-fold increase in the enrichment factor of a 23-mer pY-peptide and pY/pS normalized intensity ratios up to 1.5, when comparing the template mesoporous beads with the bulk materials.

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  • 40.
    Liu, Mingquan
    et al.
    Umeå University , Department of Chemistry, S-901 87 Umeå, Sweden.
    Tran, Tri Minh
    Umeå University , Department of Chemistry, S-901 87 Umeå, Sweden.
    Ahmed Awad, Abbas Elhaj
    Umeå University , Department of Chemistry, S-901 87 Umeå, Sweden.
    Torsetnes, Silje
    University of Southern Denmark , Department of Biochemistry & Molecular Biology and VILLUM Center for Bioanalytical Sciences, Campusvej 55, DK-5230 Odense M, Denmark.
    Jensen, Ole N.
    University of Southern Denmark , Department of Biochemistry & Molecular Biology and VILLUM Center for Bioanalytical Sciences, Campusvej 55, DK-5230 Odense M, Denmark.
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Irgum, Knut
    Umeå University , Department of Chemistry, S-901 87 Umeå, Sweden.
    Molecularly Imprinted Porous Monolithic Materials from Melamine-Formaldehyde for Selective Trapping of Phosphopeptides2017In: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 89, no 17, p. 9491-9501Article in journal (Refereed)
    Abstract [en]

    Thirty-five melamine-formaldehyde (MF) monolithic materials with bimodal pore distributions were synthesized in fused silica capillaries by catalyst-free polycondensation, starting with an aqueous MF precondensate, using acetonitrile as macroporogen and a variety of aliphatic polyethers and triblock copolymeric surfactants as porogens and mesoporogens, respectively. By varying the prepolymer composition and the type and molecular weights of the polymeric porogen components, a library of porous monolithic materials were produced, covering a range of meso- and macroporous properties. A multivariate evaluation revealed that the amount of surfactant was the strongest contributor to specific surface area and pore volume, and to the inversely related mesopore size, whereas the macropore dimension was mainly controlled by the amount of aliphatic polyether porogen. One of these capillary monoliths, chosen based on the combination of meso- and macropores providing optimal percolative flow and accessible surface area, was synthesiz¬ed in the presence of N-Fmoc and O-Et protected phosphoserine and phosphotyrosine, in order to prepare molecularly imprinted monoliths with surface layers selective for phosphopeptides. These imprinted monoliths were characterized alongside non-imprinted monoliths by a variety of techniques and finally evaluated by liquid chromatography-mass spectrometry in the capillary format to assess their abilities to trap and release phosphorylated amino acids and peptides from partly aqueous media. Selective enrichment of phosphorylated targets was demonstrated, suggesting that these materials could be useful as trapping media in affinity-based phosphoproteomics.

  • 41.
    Sulc, Robert
    et al.
    Faculty of Chemistry, Technical University of Dortmund, Germany.
    Szekely, Gyorgy
    Faculty of Chemistry, Technical University of Dortmund, Germany; Hovione FarmaCiencia SA, R&D, Lisbon, Portugal.
    Shinde, Sudhirkumar
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces. Faculty of Chemistry, Technical University of Dortmund, Germany.
    Wierzbicka, Celina
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Vilela, Filipe
    Faculty of Chemistry, Technical University of Dortmund, Germany.
    Bauer, David
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces. Faculty of Chemistry, Technical University of Dortmund, Germany.
    Phospholipid imprinted polymers as selective endotoxin scavengers2017In: Scientific Reports, E-ISSN 2045-2322, Vol. 7Article in journal (Refereed)
    Abstract [en]

    Herein we explore phospholipid imprinting as a means to design receptors for complex glycolipids comprising the toxic lipopolysaccharide endotoxin. A series of polymerizable bis-imidazolium and urea hosts were evaluated as cationic and neutral hosts for phosphates and phosphonates, the latter used as mimics of the phospholipid head groups. The bis-imidazolium hosts interacted with the guests in a cooperative manner leading to the presence of tight and well defined 1:2 ternary complexes. Optimized monomer combinations were subsequently used for imprinting of phosphatidic acid as an endotoxin dummy template. Presence of the aforementioned ternary complexes during polymerization resulted in imprinting of lipid dimers - the latter believed to crudely mimic the endotoxin Lipid A motif. The polymers were characterized with respect to template rebinding, binding affinity, capacity and common structural properties, leading to the identification of polymers which were thereafter subjected to an industrially validated endotoxin removal test. Two of the polymers were capable of removing endotoxin down to levels well below the accepted threshold (0.005 EU/mg API) in pharmaceutical production.

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  • 42.
    Bllaci, Loreta
    et al.
    Department of Biochemistry and Molecular Biology and VILLUM Center for Bioanalytical Sciences, University of Southern Denmark , DK-5230 Odense M, Denmark.
    Torsetnes, Silje
    Department of Biochemistry and Molecular Biology and VILLUM Center for Bioanalytical Sciences, University of Southern Denmark , DK-5230 Odense M, Denmark.
    Wierzbicka, Celina
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Shinde, Sudhirkumar
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Rogowska-Wrzesinska, Adelina
    Department of Biochemistry and Molecular Biology and VILLUM Center for Bioanalytical Sciences, University of Southern Denmark , DK-5230 Odense M, Denmark.
    Jensen, Ole N.
    Department of Biochemistry and Molecular Biology and VILLUM Center for Bioanalytical Sciences, University of Southern Denmark , DK-5230 Odense M, Denmark.
    Phosphotyrosine biased enrichment of tryptic peptides from cancer cells by combining pY-MIP and TiO2 affinity resins2017In: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 89, no 21, p. 11332-11340Article in journal (Refereed)
    Abstract [en]

    Protein phosphorylation at distinct tyrosine residues (pY) is essential for fast, specific, and accurate signal transduction in cells. Enrichment of pY-containing peptides derived from phosphoproteins is commonly facilitated by use of immobilized anti-pY antibodies prior to phosphoproteomics analysis by mass spectrometry. We here report on an alternative approach for pY-peptide enrichment using inexpensive pY-imprinted polymer (pY-MIP). We assessed by mass spectrometry the performance of pY-MIP for enrichment and sequencing of phosphopeptides obtained by tryptic digestion of protein extracts from HeLa cells. The combination of pY-MIP- and TiO2-based phosphopeptide enrichment provided more than 90% selectivity for phosphopeptides. Mass spectrometry signal intensities were enhanced for most pY-phosphopeptides (approximately 70%) when using the pY-MIP-TiO2 combination as compared to TiO2 alone. pY constituted up to 8% of the pY-MIP-TiO2-enriched phosphopeptide fractions. The pY-MIP-TiO2 and the TiO2 protocols yielded comparable numbers of distinct phosphopeptides, 1693 and 1842, respectively, from microgram levels of peptide samples. Detailed analysis of physicochemical properties of pY-MIP-TiO2-enriched phosphopeptides demonstrated that this protocol retrieved phosphopeptides that tend to be smaller (<24 residues), less acidic, and almost exclusively monophosphorylated, as compared to TiO2 alone. These unique properties render the pY-MIP-based phosphopeptide enrichment technique an attractive alternative for applications in phosphoproteomics research.

  • 43.
    Wan, Wei
    et al.
    Chemical and Optical Sensing Division, Bundesanstalt für Materialforschung und -prüfung (BAM), Richard-Willstätter-Strasse 11, 12489, Berlin, Germany.
    Descalzo, Ana
    Department of Organic Chemistry, Complutense University of Madrid (UCM), 28040, Madrid, Spain.
    Shinde, Sudhirkumar
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Weishoff, Hardy
    Department of Chemistry, Humboldt University Berlin, Brook-Taylor-Strasse 2, 12489, Berlin, Germany.
    Orellana, Guillermo
    Department of Organic Chemistry, Complutense University of Madrid (UCM), 28040, Madrid, Spain.
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Rurack, Knut
    Chemical and Optical Sensing Division, Bundesanstalt für Materialforschung und -prüfung (BAM), Richard-Willstätter-Strasse 11, 12489, Berlin, Germany.
    Ratiometric fluorescence detection of phosphorylated amino acids through excited‐state proton transfer using molecularly imprinted polymer (MIP) recognition nanolayers2017In: Chemistry - A European Journal, ISSN 0947-6539, E-ISSN 1521-3765, Vol. 23, no 63, p. 15974-15983Article in journal (Refereed)
    Abstract [en]

    2,3-diaminophenazine bis-urea fluorescent probe monomer (1) was developed. It responds to phenylphosphate and phosphorylated amino acids in a ratiometric fashion with enhanced fluorescence accompanied by the development of a redshifted emission band arising from an excited- state proton transfer (ESPT) process in the hydrogenbonded probe/analyte complex. The two urea groups of 1 form a cleft-like binding pocket (Kb>1010 L2mol@2 for 1:2 complex). Imprinting of 1 in presence of ethyl ester- and fluorenylmethyloxycarbonyl (Fmoc)-protected phosphorylated tyrosine (Fmoc-pTyr-OEt) as the template, methacrylamide as co-monomer, and ethyleneglycol dimethacrylate as crosslinker gave few-nanometer-thick molecularly imprinted polymer (MIP) shells on silica core microparticles with excellent selectivity for the template in a buffered biphasic assay. The supramolecular recognition features were established by spectroscopic and NMR studies. Rational screening of comonomers and cross-linkers allowed to single out the best performing MIP components, giving significant imprinting factors (IF>3.5) while retaining ESPT emission and the ratiometric response in the thin polymer shell. Combination of the bead-based detection scheme with the phase-transfer assay dramatically improved the IF to 15.9, allowing sensitive determination of the analyte directly in aqueous media.

  • 44.
    Yeung, Sing Yee
    et al.
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Mucha, Annabell
    Faculty of Chemistry, Technical University of Dortmund, Dortmund, 44227 Germany.
    Deshmukh, Ravindra
    Faculty of Chemistry, Technical University of Dortmund, Dortmund, 44227 Germany.
    Boutrus, Malak
    Faculty of Chemistry, Technical University of Dortmund, Dortmund, 44227 Germany.
    Arnebrant, Thomas
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces. Faculty of Chemistry, Technical University of Dortmund, Dortmund, 44227, Germany.
    Reversible Self-Assembled Monolayers (rSAMs): Adaptable Surfaces for Enhanced Multivalent Interactions and Ultrasensitive Virus Detection2017In: ACS Central Science, ISSN 2374-7951, Vol. 3, no 11, p. 1198-1207Article in journal (Refereed)
    Abstract [en]

    We report on the design of pH-switchable monolayers allowing a reversible and ordered introduction of affinity reagents on sensor surfaces. The principal layer building blocks consist of α-(4-amidinophenoxy)alkanes decorated at the ω-position with affinity ligands. These spontaneously self-assemble on top of carboxylic acid terminated SAMs to form reversible homo or mixed monolayers (rSAMs) that are tunable with respect to the nature of the head group, layer order and stability while featuring pH responsiveness and the dynamic nature of noncovalent build assemblies. We show that this results in a range of unique biosensor features. As a first example a sialic acid rSAM featuring strong lectin affinity is here used to sense hemagglutinin and influenza virus (H5N1) at the pM and fM level by in situ ellipsometry in a fully reversible fashion. We believe that the rSAM concept will find widespread use in surface chemistry and overall for boosting sensitivity in affinity biosensors.

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  • 45.
    Wierzbicka, Celina
    et al.
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Torsetnes, Silje
    Univ Southern Denmark, Dept Biochem & Mol Biol, Odense, Denmark.
    Jensen, Ole
    Shinde, Sudhirkumar
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Surface imprinted phosphopeptide capture beads2017In: Abstracts of Papers of the American Chemical Society, ISSN 0065-7727, Vol. 253Article in journal (Other academic)
  • 46.
    Chen, Zhiliang
    et al.
    Key Laboratory of Environment and Health, Ministry of Education & Ministry of Environmental Protection and State Key Laboratory of Environmental Health (Incubation), School of Public Health, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Shen, Xiantao
    Key Laboratory of Environment and Health, Ministry of Education & Ministry of Environmental Protection and State Key Laboratory of Environmental Health (Incubation), School of Public Health, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
    Synergistic Catalysis by “Polymeric Microzymes and Inorganic Nanozymes”: The 1+1>2 Effect for Intramolecular Cyclization of Peptides2017In: Frontiers in Chemistry, E-ISSN 2296-2646, Vol. 5, article id 60Article in journal (Refereed)
    Abstract [en]

    In this work, we developed an efficient “molecularly imprinted polymer microzymes and inorganic magnetic nanozymes” synergistic catalysis strategy for the formation of disulfide bonds in peptides. The polymeric microzymes showed excellent selectivity toward the template peptide as well as the main reactant (linear peptide), and the Fe3O4 magnetic nanoparticle (MNP) nanozymes inhibited the intermolecular reaction during the formation of disulfide bonds in peptides. As a result, the integration of the two different artificial enzymes in one process facilitates the intramolecular cyclization in high product yields (59.3%) with excellent selectivity. Mechanism study indicates the synergistic effect was occurred by using a “reversed solid phase synthesis” strategy with an enhanced shift of reaction balance to product generation. We believe the synergistic catalysis by “polymeric microzymes and inorganic nanozymes” presented in the present work may open new opportunities in creation of multifunctional enzyme mimics for sensing, imaging, and drug delivery.

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  • 47.
    Shen, Xiantao
    et al.
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces. Key Laboratory of Environment and Health, Ministry of Education & Ministry of Environmental Protection, State Key Laboratory of Environmental Health (Incubation), School of Public Health, Tongji Medical College, Huazhong University of Science and Technology , Hangkong Road #13, Wuhan, Hubei 430030, China; G&T Septech AS , P.O. Box 33, 1917 Ytre Enebakk, Norway.
    Huang, Chuixiu
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Shinde, Sudhirkumar
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Jagadeesan, Kishore
    Department of Biomedical Engineering, Lund University , 221 00 Lund, Sweden.
    Ekström, Simon
    Department of Biomedical Engineering, Lund University , 221 00 Lund, Sweden.
    Fritz, Emelie
    INFU, Technische Universität Dortmund , 44221 Dortmund, Germany.
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Catalytic Formation of Disulfide Bonds in Peptides by Molecularly Imprinted Microgels at Oil/Water Interfaces2016In: ACS Applied Materials and Interfaces, ISSN 1944-8244, E-ISSN 1944-8252, Vol. 8, no 44, p. 30484-30491Article in journal (Refereed)
    Abstract [en]

    This work describes the preparation and investigation of molecularly imprinted polymer (MIP) microgels (MGs) stabilized Pickering emulsions (PE) for their ability to catalyze the formation of disulfide bonds in peptides at the O/W interface. The MIP MGs were synthesized via precipitation polymerization and a programmed initiator change strategy. The MIP MGs were characterized using DLS analysis, SEM measurement and optical microscopy analysis. The dry and wet MIP MGs showed a hydrodynamic diameter of 100 nm and 280 nm, respectively. Template rebinding experiment showed that the MIP MGs bound over two times more template (24 mg g-1) compared to the uptake displayed by a non-imprinted reference polymer (NIP) MG (10 mg g-1) at saturation. Using the MIP MGs as stabilizers, catalytic oxidation systems were prepared by emulsifying the oil phase and water phase in presence of different oxidizing agents. During the cyclization, the isolation of the thiol precursors and the oxidizing reagents non-selectively decreased the formation of the byproducts, while the imprinted cavities on the MIP MGs selectively promoted the intramolecular cyclization of peptides. When I2 was used as the oxidizing agent, the MIP-PE-I2 system showed a product yield of 50 %, corresponding to a nearly two-fold increase compared to the non-imprinted polymer NIP-PE-I2 system (26 %). We believe the interfacial catalysis system presented in this work may offer significant benefits in synthetic peptide chemistry by raising productivity while suppressing the formation of by-products.

  • 48.
    El-Schich, Zahra
    et al.
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Abdullah, Mohammad
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Shinde, Sudhirkumar
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Dizeyi, Nishtman
    Department of Translational Medicine, Lund University, Malmö, Sweden.
    Rosén, Anders
    Department of Clinical and Experimental Medicine, Division of Cell Biology, Linköping University, Linköping, Sweden.
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Gjörloff Wingren, Anette
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Different expression levels of glycans on leukemic cells-a novel screening method with molecularly imprinted polymers (MIP) targeting sialic acid2016In: Tumor Biology, ISSN 1010-4283, E-ISSN 1423-0380, Vol. 10, no 37, p. 13763-13768Article in journal (Refereed)
    Abstract [en]

    Sialic acid (SA) is normally expressed on the cell membranes and is located at the terminal position of the sugar chains. SA plays an important role for regulation of the innate immunity, function as markers of the cells and can be recognized by a variety of receptors. Interestingly, the level of SA expression is increased on metastatic cancer cells. The availability of specific antibodies against SA is limited and, therefore, biomarker tools for detection of SA are lacking. We have recently presented a novel method for specific fluorescence labeling of SA molecular imprinted polymers (MIP). Here, we have performed an extended screening of SA expression by using SA-MIP and included four different chronic lymphocytic leukemia (CLL) cell lines, conveniently analyzed by flow cytometry and fluorescence microscopy. SA expression was detected in four cell lines at different levels, and the SA expression were verified with lectin-FITC. These results show that SA-MIP can be used as a plastic antibody for detection of SA using both flow cytometry and fluorescence microscopy. We suggest that SA-MIP can be used for screening of different tumor cells of various stages, including CLL cells.

  • 49.
    Gutierrez Climente, Raquel
    et al.
    Department of Analytical Chemistry, Faculty of Pharmacy, University of the Basque Country, Vitoria-Gasteiz (Álava), Spain.
    Gomez Caballero, Alberto
    Department of Analytical Chemistry, Faculty of Pharmacy, University of the Basque Country, Vitoria-Gasteiz (Álava), Spain.
    Halhalli, Mahadeo
    INFU, Faculty of Chemistry, Technical University of Dortmund, Dortmund, Germany.
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Goicolea, Aranzazu
    Department of Analytical Chemistry, Faculty of Pharmacy, University of the Basque Country, Vitoria-Gasteiz (Álava), Spain.
    Barrio, Ramon J
    Department of Analytical Chemistry, Faculty of Pharmacy, University of the Basque Country, Vitoria-Gasteiz (Álava), Spain.
    Iniferter-mediated grafting of molecularly imprinted polymers on porous silica beads for the enantiomeric resolution of drugs2016In: Journal of Molecular Recognition, ISSN 0952-3499, E-ISSN 1099-1352, Vol. 29, no 3, p. 106-114Article in journal (Refereed)
    Abstract [en]

    A surface-imprinted chiral stationary phase for the enantiomeric resolution of the antidepressant drug, citalopram, is presented in this work. N, N'-diethylaminodithiocarbamoylpropyl(trimethoxy)silane has been used as silane iniferter for the surface functionalization of the solid silica support. A molecularly imprinted polymer thin film, in the nm scale, was then grafted on the silanized silica using itaconic acid as the functional monomer and ethylene glycol dimethacrylate as the cross-linker in the presence of the template S-citalopram. The total monomer amount was calculated to obtain the desired thickness. Non-imprinted stationary phases were prepared similarly in the absence of S-citalopram. Characterization of the materials was carried out by scanning electron microscopy, thermogravimetric analysis, elemental analysis and Fourier transform infrared spectroscopy. Stationary phases have been applied to the chromatographic separation of the target. Conditions for best chromatographic resolution of the enantiomers were optimized, and it was found that a mobile phase consisting of a mixture of formate buffer (40 mM, pH 3) and acetonitrile (30:70 v/v) at 40 °C provided best results. Binding behaviour of the developed material was finally assessed by batch rebinding experiments. The obtained binding isotherm was fitted to different binding models being the Freundlich-Langmuir model, the one that best fitted the experimental data. The developed material has shown high selectivity for the target enantiomer, and the stationary phase could be undoubtedly exploited for chiral separation of the drug.

  • 50.
    Wang, Jixiang
    et al.
    School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang, Jiangsu 212013, China.
    Qiu, Hao
    School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang, Jiangsu 212013, China.
    Shen, Hongqiang
    School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang, Jiangsu 212013, China.
    Pan, Jianming
    School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang, Jiangsu 212013, China.
    Dai, Xiaohui
    School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang, Jiangsu 212013, China.
    Yan, Yongsheng
    School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang, Jiangsu 212013, China.
    Pan, Guoqing
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces. Department of Orthopaedics, The First Affiliated Hospital of Soochow University, Orthopaedic Institute, Soochow University, 188 Shizi Street, Suzhou, Jiangsu 215006, China.
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Molecularly Imprinted Fluorescent Hollow Nanoparticles as Sensors for Rapid and Efficient Detection λ-Cyhalothrin in Environmental Water2016In: Biosensors & bioelectronics, ISSN 0956-5663, E-ISSN 1873-4235, Vol. 85, p. 387-394Article in journal (Refereed)
    Abstract [en]

    Molecularly imprinted fluorescent polymers have shown great promise in biological or chemical separations and detections, due to their high stability, selectivity and sensitivity. In this work, molecularly imprinted fluorescent hollow nanoparticles, which could rapidly and efficiently detect λ-cyhalothrin (a toxic insecticide) in water samples, was reported. The molecularly imprinted fluorescent sensor showed excellent sensitivity (the limit of detection low to 10.26 nM), rapid detection rate (quantitative detection of λ-cyhalothrin within 8 min), regeneration ability (maintaining good fluorescence properties after 8 cycling operation) and appreciable selectivity over several structural analogues. Moreover, the fluorescent sensor was further used to detect λ-cyhalothrin in real samples form the Beijing-Hangzhou Grand Canal Water. Despite the relatively complex components of the environmental water, the molecularly imprinted fluorescent hollow nanosensor still showed good recovery, clearly demonstrating the potential value of this smart sensor nanomaterial in environmental monitoring.

12 1 - 50 of 77
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