Publikationer från Malmö universitet
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  • 1.
    Mavliutova, Liliia
    et al.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Munoz Aldeguer, Bruna
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Wiklander, Jesper
    Linnaeus University.
    Wierzbicka, Celina
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Huynh, Chau Minh
    Umeå University.
    Nicholls, Ian A.
    Linnaeus University.
    Irgum, Knut
    Umeå University.
    Sellergren, Börje
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Discrimination between sialic acid linkage modes using sialyllactose-imprinted polymers2021Inngår i: RSC Advances, E-ISSN 2046-2069, Vol. 11, nr 36, s. 22409-22418Artikkel i tidsskrift (Fagfellevurdert)
    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 universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Verduci, Elena
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Sellergren, Börje
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Combinatorial design of a sialic acid imprinted binding site exploring a dual ion receptor approach2021Inngår i: RSC Advances, E-ISSN 2046-2069, Vol. 11, nr 54, artikkel-id 34329Artikkel i tidsskrift (Fagfellevurdert)
    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.
    Department of Chemistry, University of Oslo 0315 Oslo Norway.
    König, Nico
    Department of Chemistry, University of Oslo 0315 Oslo Norway; Jülich Centre for Neutron Science (JCNS) and Institute for Complex Systems (ICS), Forschungszentrum Jülich GmbH 52425 Jülich Germany.
    Yang, Su
    Department of Chemistry & Biochemistry, The University of Texas at Arlington Arlington Texas 76019 USA.
    Skoda, Maximilian W. A.
    ISIS Pulsed Neutron and Muon Source, Science and Technology Facilities Council, Rutherford Appleton Laboratory Harwell Science and Innovation Campus, Didco Oxfordshire OX11 OQX UK.
    Maestro, Armando
    Institut Laue - Langevin 38000 Grenoble France.
    He, Dong
    Department of Chemistry & Biochemistry, The University of Texas at Arlington Arlington Texas 76019 USA.
    Cárdenas, Marité
    Malmö universitet, Biofilms Research Center for Biointerfaces. Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Lund, Reidar
    Department of Chemistry, University of Oslo 0315 Oslo Norway.
    Lipid membrane interactions of self-assembling antimicrobial nanofibers: effect of PEGylation2020Inngår i: RSC Advances, E-ISSN 2046-2069, Vol. 10, s. 35329-35340, artikkel-id 35329Artikkel i tidsskrift (Fagfellevurdert)
    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, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Engineering Enzymology, A.N. Bach Institute of Biochemistry, Moscow, 119 071, Russian Federation; Kurchatov NBICS Centre, National Research Centre Kurchatov Institute, Moscow, 123182, Russian Federation.
    Ohlsson, Lars
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Gudmundsson, Petri
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Halak, Sanela
    Medical Imaging and Physiology, Skåne University Hospital, Malmö, 205 06, Sweden.
    Ljunggren, Lennart
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Blum, Zoltan
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Shleev, Sergey
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Engineering Enzymology, A.N. Bach Institute of Biochemistry, Moscow, 119 071, Russian Federation; Kurchatov NBICS Centre, National Research Centre Kurchatov Institute, Moscow, 123182, Russian Federation.
    Ex vivo electric power generation in human blood using an enzymatic fuel cell in a vein replica2016Inngår i: RSC Advances, E-ISSN 2046-2069, Vol. 6, nr 74, s. 70215-70220Artikkel i tidsskrift (Fagfellevurdert)
    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.

    Fulltekst (pdf)
    FULLTEXT01
  • 5.
    Pankratov, Dmitry
    et al.
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Sundberg, Richard
    Suyatin, Dmitry B.
    Sotres, Javier
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Barrantes, Alejandro
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Ruzgas, Tautgirdas
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Maximov, Ivan
    Montelius, Lars
    Shleev, Sergey
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    The influence of nanoparticles on enzymatic bioelectrocatalysis2014Inngår i: RSC Advances, E-ISSN 2046-2069, Vol. 4, nr 72, s. 38164-38168Artikkel i tidsskrift (Fagfellevurdert)
    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.

    Fulltekst (pdf)
    FULLTEXT01
  • 6.
    Schwark, Sebastian
    et al.
    Lehrstuhl für Technische Chemie II, Universität Duisburg-Essen, Essen, Germany.
    Sun, Wei
    Faculty of Chemistry, Technical University of Dortmund, Germany.
    Stute, Jörg
    Bibitec GmbH, Bielefeld, Germany.
    Lütkemeyer, Dirk
    Bibitec GmbH, Bielefeld, Germany.
    Ulbricht, Mathias
    Lehrstuhl für Technische Chemie II, Universität Duisburg-Essen, Essen, Germany.
    Sellergren, Börje
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Faculty of Chemistry, Technical University of Dortmund, Germany.
    Monoclonal antibody capture from cell culture supernatants using epitope imprinted macroporous membranes2016Inngår i: RSC Advances, E-ISSN 2046-2069, Vol. 6, nr 58, s. 53162-53169Artikkel i tidsskrift (Fagfellevurdert)
    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.

    Fulltekst (pdf)
    FULLTEXT01
  • 7.
    Shen, Xiantao
    et al.
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). 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; GandT Septech, AS Verkstedveien 29, Ski, 1400, Norway.
    Huang, Chuixiu
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). School of Pharmacy, University of Oslo, PO Box 1068, Blindern, Oslo, 0316, Norway; GandT Septech, AS Verkstedveien 29, Ski, 1400, Norway.
    Shinde, Sudhirkumar
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Switnicka-Plak, Magdalena
    Department of Pure and Applied Chemistry, University of Strathclyde, Thomas Graham Building, 295 Cathedral Street, Glasgow, G1 1XL, United Kingdom.
    Cormack, Peter A.G.
    Department of Pure and Applied Chemistry, University of Strathclyde, Thomas Graham Building, 295 Cathedral Street, Glasgow, G1 1XL, United Kingdom.
    Sellergren, Börje
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Reflux precipitation polymerization: A new synthetic insight in molecular imprinting at high temperature2016Inngår i: RSC Advances, E-ISSN 2046-2069, nr 85, s. 81458-81461Artikkel i tidsskrift (Fagfellevurdert)
    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.
    College of Chemistry, Nanchang University Nanchang Jiangxi 330031 China.
    Ling, Baoping
    School of Chemistry and Chemical Engineering, Qufu Normal University Qufu Shandong 273165 China.
    Li, Qianjin
    Department of Food Science and Engineering, School of Food Science and Pharmaceutical Engineering, Nanjing Normal University Nanjing 210023 China.
    Abouhany, Rahma
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Dual roles of 3-aminopropyltriethoxysilane in preparing molecularly imprinted silica particles for specific recognition of target molecules2020Inngår i: RSC Advances, E-ISSN 2046-2069, Vol. 10, nr 34, s. 20368-20373Artikkel i tidsskrift (Fagfellevurdert)
    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.

    Fulltekst (pdf)
    fulltext
  • 9.
    Wierzbicka, Celina
    et al.
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (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, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Sellergren, Börje
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Hierarchically templated beads with tailored pore structure for phosphopeptide capture and phosphoproteomics2017Inngår i: RSC Advances, E-ISSN 2046-2069, Vol. 7, nr 28, s. 17154-17163Artikkel i tidsskrift (Fagfellevurdert)
    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.

    Fulltekst (pdf)
    FULLTEXT01
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