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  • 1.
    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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  • 2.
    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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  • 3. Nielsen, Josefine Eilsø
    et al.
    König, Nico
    Yang, Su
    Skoda, Maximilian W. A.
    Maestro, Armando
    He, Dong
    Cárdenas, Marité
    Malmö University, Biofilms Research Center for Biointerfaces. Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Lund, Reidar
    Lipid membrane interactions of self-assembling antimicrobial nanofibers: effect of PEGylation2020In: RSC Advances, E-ISSN 2046-2069, Vol. 10, p. 35329-35340, article id 35329Article in journal (Refereed)
    Abstract [en]

    Supramolecular assembly and PEGylation (attachment of a polyethylene glycol polymer chain) of peptides can be an effective strategy to develop antimicrobial peptides with increased stability, antimicrobial efficacy and hemocompatibility. However, how the self-assembly properties and PEGylation affect their lipid membrane interaction is still an unanswered question. In this work, we use state-of-the-art small angle X-ray and neutron scattering (SAXS/SANS) together with neutron reflectometry (NR) to study the membrane interaction of a series of multidomain peptides, with and without PEGylation, known to self-assemble into nanofibers. Our approach allows us to study both how the structure of the peptide and the membrane are affected by the peptide–lipid interactions. When comparing self-assembled peptides with monomeric peptides that are not able to undergo assembly due to shorter chain length, we found that the nanofibers interact more strongly with the membrane. They were found to insert into the core of the membrane as well as to absorb as intact fibres on the surface. Based on the presented results, PEGylation of the multidomain peptides leads to a slight net decrease in the membrane interaction, while the distribution of the peptide at the interface is similar to the non-PEGylated peptides. Based on the structural information, we showed that nanofibers were partially disrupted upon interaction with phospholipid membranes. This is in contrast with the considerable physical stability of the peptide in solution, which is desirable for an extended in vivo circulation time.

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  • 4.
    Pankratov, Dmitry
    et al.
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Ohlsson, Lars
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Gudmundsson, Petri
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Halak, Sanela
    Ljunggren, Lennart
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Blum, Zoltan
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Shleev, Sergey
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Ex vivo electric power generation in human blood using an enzymatic fuel cell in a vein replica2016In: RSC Advances, E-ISSN 2046-2069, Vol. 6, no 74, p. 70215-70220Article in journal (Refereed)
    Abstract [en]

    Here we report an enzymic fuel cell in a vein replica that generates sustained electricity, enough to power an e-​ink display, in an authentic human blood stream. We also detail a simple and safe approach for fuel cell evaluation under homeostatic conditions. Our results demonstrate proof-​of-​principle operation of a biocompatible and safe biodevice that could be implanted in superficial human veins, which we anticipate to be a starting point for more sophisticated investigations of personal sources of electricity.

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  • 5.
    Pankratov, Dmitry
    et al.
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Sundberg, Richard
    Suyatin, Dmitry B.
    Sotres, Javier
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Barrantes, Alejandro
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Ruzgas, Tautgirdas
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Maximov, Ivan
    Montelius, Lars
    Shleev, Sergey
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    The influence of nanoparticles on enzymatic bioelectrocatalysis2014In: RSC Advances, E-ISSN 2046-2069, Vol. 4, no 72, p. 38164-38168Article in journal (Refereed)
    Abstract [en]

    In nearly all papers concerning enzyme–nanoparticle based bioelectronic devices, it is stated that the presence of nanoparticles on electrode surfaces per se enhances bioelectrocatalysis, although the reasons for that enhancement are often unclear. Here, we report detailed experimental evidence that neither an overpotential of bioelectrocatalysis, nor direct electron transfer and bioelectrocatalytic reaction rates for an adsorbed enzyme depend on the size of nanoparticles within the range of 20–80 nm, i.e. for nanoparticles that are considerably larger than the enzyme molecules.

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  • 6. Schwark, Sebastian
    et al.
    Sun, Wei
    Stute, Jörg
    Lütkemeyer, Dirk
    Ulbricht, Mathias
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Monoclonal antibody capture from cell culture supernatants using epitope imprinted macroporous membranes2016In: RSC Advances, E-ISSN 2046-2069, Vol. 6, no 58, p. 53162-53169Article in journal (Refereed)
    Abstract [en]

    Epitope-imprinted membranes targeting the C-terminal fragment of the immunoglobuline G (IgG) heavy chain was developed and used for the purification of a commercial monoclonal antibody. The membranes exhibited strongly enhanced IgG affinity when compared with non-imprinted or IgG imprinted membranes reflected in binding selectivities in a protein mixture (IgG/HSA 1 : 10 w/w) of up to 40, and the elution of 95 to 100% pure IgG after washing. The dynamic binding capacity amounted to 3.9 mg mL(-1) membrane volume with minor loss in performance upon repeated cleaning with alkali. The depletion of host cell proteins from a cell culture broth after production of anti-IL8 antibody using the best performing imprinted membrane under low-salt conditions reached 88% (0.7-1.2 log units) implying an effective removal of impurities from the cell culture supernatant.

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  • 7.
    Shen, Xiantao
    et al.
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Huang, Chuixiu
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Shinde, Sudhirkumar
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Switnicka-Plak, Magdalena
    Cormack, Peter A.G.
    Sellergren, Börje
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Reflux precipitation polymerization: A new synthetic insight in molecular imprinting at high temperature2016In: RSC Advances, E-ISSN 2046-2069, no 85, p. 81458-81461Article in journal (Refereed)
    Abstract [en]

    The synthesis of uniform molecularly imprinted polymer (MIP) microspheres (MSs) using distillation precipitation polymerization (DPP) at high temperature has attracted great interest in the field of molecular imprinting. However, there are still some shortcomings in this method. In this work, to create uniform MIP MSs in a short time and to demonstrate the effects of high temperature on imprinting performance, a new precipitation polymerization method (reflux precipitation polymerization, RPP) was used for the first time to fabricate MIP MSs in this study. The SEM images of the polymeric MSs indicate the presence of template molecules could improve the particle morphology and size uniformity. The specific molecular recognition of the monodispersed MIP MSs was confirmed by fluorescence measurement and HPLC-UV analysis. The binding behavior of the MIP MSs was simulated using the heterogeneous Freundlich isotherm, which shows that the MIP MSs produced by the RPP possess compatible selectivity in comparison with those produced by traditional PP method. It is noted that, for the first time, we demonstrated that molecular imprinting at high temperature was only successful when electrostatic interactions played important roles in the imprinting process.

  • 8. Wang, Fenying
    et al.
    Ling, Baoping
    Li, Qianjin
    Abouhany, Rahma
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Dual roles of 3-aminopropyltriethoxysilane in preparing molecularly imprinted silica particles for specific recognition of target molecules2020In: RSC Advances, E-ISSN 2046-2069, Vol. 10, no 34, p. 20368-20373Article in journal (Refereed)
    Abstract [en]

    3-Aminopropyltriethoxysilane (APTES) is a silane widely used to supply amino groups for further modifications on various materials, but it is less studied as a catalyst to catalyze sol-gel silica polymerization. Here, by using APTES as the catalyst instead of the conventional basic catalysts, a novel strategy was developed to prepare silica-based molecularly imprinted polymers (MIPs). Meanwhile, APTES was employed as the functional monomer to create imprinted nanocavities for specific recognition of target molecules. The as-synthesized MIP exhibited ultra-high recognition capability due to the elimination of the detrimental effect on the imprinting performance caused by the additional catalysts. The preparation process, specificity, pH effect, binding capacity and affinity of the MIP were studied in detail. The MIP microparticles could be packed into a solid phase extraction column for removing the target molecule in water efficiently, and the molecule could easily be enriched by 40 times. The interaction of the functional monomer and template was studied by the calculation method, giving a more clear understanding of the recognition behaviours of the imprinted polymers. The strategy could be extended not only to prepare highly specific MIPs for other small phosphoric molecules, but also for biomolecules e.g. phosphorylated peptides or proteins.

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  • 9.
    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.
    Jensen, Ole N.
    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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