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  • 1.
    Aleksejeva, Olga
    et al.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Nilsson, N.
    Obducat Technol AB, S-22363 Lund, Sweden..
    Genevskiy, Vladislav
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Thulin, K.
    Obducat Technol AB, S-22363 Lund, Sweden..
    Shleev, Sergey
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Dual-feature photobioanodes based on nanoimprint lithography for photoelectric biosupercapacitors2022Ingår i: Journal of Power Sources, ISSN 0378-7753, E-ISSN 1873-2755, Vol. 517, artikel-id 230677Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Direct transformation of solar energy into electrical energy by means of biological photosynthesis is considered as an attractive option for sustainable electrical energy production. Thylakoid membranes, the site of photosynthesis, are regarded as a promising biological material for the development of photoelectric biodevices, which produce electrical power consuming only light energy as oxygen evolves at photobioanode upon irradiation and biocathode converts it back to water. Therefore, in this work dual-feature photobioanode based on nanoimprinted gold substrates modified with thylakoids in combination with a capacitive part made of a planar gold substrate coated with a conductive polymer was designed and evaluated, providing open-circuit potential of -0.21 V vs. Ag vertical bar AgCl vertical bar KClsat and a capacitance of ca. 60 F m(-2) both at ambient light and artificial illumination of 400 W m(-2). Combination of thylakoid based dual-feature photobioanode with bilirubin oxidase modified transparent and capacitive indium tin oxide biocathode resulted in a photoelectric biosupercapacitor with remarkable characteristics at ambient light, viz. an open-circuit voltage as high as 0.74 V, which was stable upon charge-discharge cycles during ca. 2 h.

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  • 2.
    Beck, Christian
    et al.
    Institut für Angewandte Physik, Universität Tübingen, Auf der Morgenstelle 10, 72076 Tübingen, Germany; Institut Max von Laue─Paul Langevin (ILL), CS 20156, F-38042 Grenoble Cedex 9, France.
    Grimaldo, Marco
    Institut Max von Laue─Paul Langevin (ILL), CS 20156, F-38042 Grenoble Cedex 9, France.
    Lopez, Hender
    School of Physics and Optometric & Clinical Sciences, Technological University Dublin, D07 XT95 Grangegorman, Ireland.
    Da Vela, Stefano
    Institut für Angewandte Physik, Universität Tübingen, Auf der Morgenstelle 10, 72076 Tübingen, Germany.
    Sohmen, Benedikt
    Institut für Angewandte Physik, Universität Tübingen, 72076 Tübingen, Germany.
    Zhang, Fajun
    Institut für Angewandte Physik, Universität Tübingen, Auf der Morgenstelle 10, 72076 Tübingen, Germany.
    Oettel, Martin
    Institut für Angewandte Physik, Universität Tübingen, Auf der Morgenstelle 10, 72076 Tübingen, Germany.
    Barrat, Jean-Louis
    Univ. Grenoble Alpes, CNRS, LiPhy, 38000 Grenoble, France.
    Roosen-Runge, Felix
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Schreiber, Frank
    Institut für Angewandte Physik, Universität Tübingen, Auf der Morgenstelle 10, 72076 Tübingen, Germany.
    Seydel, Tilo
    Institut Max von Laue─Paul Langevin (ILL), CS 20156, F-38042 Grenoble Cedex 9, France.
    Short-Time Transport Properties of Bidisperse Suspensions of Immunoglobulins and Serum Albumins Consistent with a Colloid Physics Picture.2022Ingår i: Journal of Physical Chemistry B, ISSN 1520-6106, E-ISSN 1520-5207, Vol. 126, nr 38, s. 7400-7408Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The crowded environment of biological systems such as the interior of living cells is occupied by macromolecules with a broad size distribution. This situation of polydispersity might influence the dependence of the diffusive dynamics of a given tracer macromolecule in a monodisperse solution on its hydrodynamic size and on the volume fraction. The resulting size dependence of diffusive transport crucially influences the function of a living cell. Here, we investigate a simplified model system consisting of two constituents in aqueous solution, namely, of the proteins bovine serum albumin (BSA) and bovine polyclonal gamma-globulin (Ig), systematically depending on the total volume fraction and ratio of these constituents. From high-resolution quasi-elastic neutron spectroscopy, the separate apparent short-time diffusion coefficients for BSA and Ig in the mixture are extracted, which show substantial deviations from the diffusion coefficients measured in monodisperse solutions at the same total volume fraction. These deviations can be modeled quantitatively using results from the short-time rotational and translational diffusion in a two-component hard sphere system with two distinct, effective hydrodynamic radii. Thus, we find that a simple colloid picture well describes short-time diffusion in binary mixtures as a function of the mixing ratio and the total volume fraction. Notably, the self-diffusion of the smaller protein BSA in the mixture is faster than the diffusion in a pure BSA solution, whereas the self-diffusion of Ig in the mixture is slower than in the pure Ig solution.

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  • 3.
    Beyer, Sarah
    et al.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Kimani, Martha
    Chemical and Optical Sensing Division, Bundesanstalt für Materialforschung und -prüfung (BAM), Richard-Willstätter Straße 11, 12489 Berlin, Germany.
    Zhang, Yuecheng
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Verhassel, Alejandra
    Institute of Biomedicine, University of Turku, 20520 Turku, Finland; FICAN West Cancer Centre, Turku University Hospital, 20520 Turku, Finland.
    Sternbæk, Louise
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces. Phase Holographic Imaging AB, SE-223 63 Lund, Sweden.
    Wang, Tianyan
    Department of Molecular Biology, Umeå University, SE-901 87 Umeå, Sweden.
    Persson, Jenny L.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces. Department of Molecular Biology, Umeå University, SE-901 87 Umeå, Sweden.
    Härkönen, Pirkko
    Institute of Biomedicine, University of Turku, 20520 Turku, Finland; FICAN West Cancer Centre, Turku University Hospital, 20520 Turku, Finland.
    Johansson, Emil
    Department of Chemistry, Umeå University, SE-901 87 Umeå, Sweden; Umeå Centre for Microbial Research, Umeå University, SE-901 87 Umeå, Sweden.
    Caraballo, Remi
    Department of Chemistry, Umeå University, SE-901 87 Umeå, Sweden; Umeå Centre for Microbial Research, Umeå University, SE-901 87 Umeå, Sweden.
    Elofsson, Mikael
    Department of Chemistry, Umeå University, SE-901 87 Umeå, Sweden; Umeå Centre for Microbial Research, Umeå University, SE-901 87 Umeå, Sweden.
    Gawlitza, Kornelia
    Chemical and Optical Sensing Division, Bundesanstalt für Materialforschung und -prüfung (BAM), Richard-Willstätter Straße 11, 12489 Berlin, Germany.
    Rurack, Knut
    Chemical and Optical Sensing Division, Bundesanstalt für Materialforschung und -prüfung (BAM), Richard-Willstätter Straße 11, 12489 Berlin, Germany.
    Ohlsson, Lars
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    El-Schich, Zahra
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Gjörloff Wingren, Anette
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Stollenwerk, Maria M
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Fluorescent Molecularly Imprinted Polymer Layers against Sialic Acid on Silica-Coated Polystyrene Cores-Assessment of the Binding Behavior to Cancer Cells.2022Ingår i: Cancers, ISSN 2072-6694, Vol. 14, nr 8, artikel-id 1875Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Sialic acid (SA) is a monosaccharide usually linked to the terminus of glycan chains on the cell surface. It plays a crucial role in many biological processes, and hypersialylation is a common feature in cancer. Lectins are widely used to analyze the cell surface expression of SA. However, these protein molecules are usually expensive and easily denatured, which calls for the development of alternative glycan-specific receptors and cell imaging technologies. In this study, SA-imprinted fluorescent core-shell molecularly imprinted polymer particles (SA-MIPs) were employed to recognize SA on the cell surface of cancer cell lines. The SA-MIPs improved suspensibility and scattering properties compared with previously used core-shell SA-MIPs. Although SA-imprinting was performed using SA without preference for the α2,3- and α2,6-SA forms, we screened the cancer cell lines analyzed using the lectins Maackia Amurensis Lectin I (MAL I, α2,3-SA) and Sambucus Nigra Lectin (SNA, α2,6-SA). Our results show that the selected cancer cell lines in this study presented a varied binding behavior with the SA-MIPs. The binding pattern of the lectins was also demonstrated. Moreover, two different pentavalent SA conjugates were used to inhibit the binding of the SA-MIPs to breast, skin, and lung cancer cell lines, demonstrating the specificity of the SA-MIPs in both flow cytometry and confocal fluorescence microscopy. We concluded that the synthesized SA-MIPs might be a powerful future tool in the diagnostic analysis of various cancer cells.

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  • 4.
    Buchanan, Claire
    et al.
    Department of Chemistry and Physics, La Trobe University, Bundoora, Australia.
    Garvey, Christopher J.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces. Australian Nuclear Science and Technology Organization (ANSTO), Lucas Heights, Australia; Lund Institute for Advanced Neutron and X-ray Science (LINXS), Lund, Sweden.
    Puskar, Ljiljana
    Helmholtz Zentrum Berlin für Materialien und Energie GmbH, Berlin, Germany.
    Perlmutter, Patrick
    Department of Chemistry and Physics, La Trobe University, Bundoora, Australia.
    Mechler, Adam
    Department of Chemistry and Physics, La Trobe University, Bundoora, Australia.
    Coordination crosslinking of helical substituted oligoamide nanorods with Cu(II)2020Ingår i: Supramolecular chemistry (Print), ISSN 1061-0278, E-ISSN 1029-0478, Vol. 32, nr 3, s. 222-232Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Substituted oligoamides are short sequences of unnatural amino acids. Oligoamides made entirely of beta(3) amino acids yield helical monomers that, if N-acylated, assemble into nanorod structures via a supramolecular assembly motif. In this work, coordination crosslinking was used to create complex nanomaterials from oligoamides WKLWEL (KE) and WELWEL (EE) (the letters denote the analogous alpha-amino acids). Upon Cu(II) addition, atomic force microscopy and small angle neutron scattering revealed morphologic changes specific to KE but absent in EE. Vibration spectroscopy measurements revealed that Cu(II) can coordinate to the amine moieties of the side chains, without direct effect on the backbone amides. While coordination in excess solvent lead to regular nanostructures, fast drying of the sample yielded oligoamide templated crystallization of CuCl2. The metal coordination crosslinking of supramolecular assemblies as reported here is the first realization of a metallosupramolecular framework structure. [GRAPHICS] .

  • 5.
    Buchanan, Claire
    et al.
    La Trobe Univ, Dept Chem & Phys, Bundoora, Vic, Australia..
    Hinds, Mark G.
    Univ Melbourne, Bio21 Mol Sci & Biotechnol Inst, Parkville, Vic, Australia..
    Puskar, Ljiljana
    Helmholtz Zentrum Berlin Mat & Energie GmbH, Berlin, Germany..
    Garvey, Christopher J.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces. Lund Inst Adv Neutron & Xray Sci, S-22370 Lund, Sweden..
    Mechler, Adam
    La Trobe Univ, Dept Chem & Phys, Bundoora, Vic, Australia..
    Comprehensive multidimensional study of the self-assembly properties of a three residue substituted beta(3) oligoamide2021Ingår i: Pure and Applied Chemistry, ISSN 0033-4545, E-ISSN 1365-3075, Vol. 93, nr 11, s. 1327-1341Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Substituted (beta(3) oligoamides form a unique self-assembling system where each monomer folds into a helix containing approximately three (beta(3) amino acids per turn, yielding a geometrically well-defined cylindrical building block that, when N-acylated, is able to self-assemble head-to-tail into nanorods that can reach several 100 mu m length. It was shown in previous works that self-assembly can be achieved with a three residue long oligoamide as well that lacks any intramolecular H-bonds, yet it crystallizes in a helix-like conformation. The self-assembly properties of these small oligoamides are however elusive, suggesting a more complex system than the self-assembly of the H-bond stabilized helical monomers. Here we focus on the self-assembly behaviour of a three residue oligoamide, Ac-beta(3)[LIA] where the letters denote the side chain of the analogous a amino acid. Ac-beta(3)[LIA] can yield highly inhomogeneous suspensions in water with a broad range of large fibrous structures that seem to be very stable, yet occasionally fibre growth is only observed upon heating. The small size of the monomer suggests a highly dynamic equilibrium yet all previous attempts failed to clearly identify low molecular weight species. Therefore a special methodology was employed in this study to characterize the suspensions at different size ranges: SANS that is optimal to measure the small oligomers and cross sectional diameter of the assemblies, DLS that is sensitive to the large populations and therefore the length of the superstructures, and NMR that is sensitive to monomeric and small oligomeric form, in conjunction with IR spectroscopy to probe the folding and AFM to image the morphology of the assemblies. Temperature ramping was used to perturb the system to probe the dynamicity of the self-assembly. It was found that the anomalous self-assembly behaviour of Ac-beta(3)[LIA] is caused by its two stable conformations, a helix-building "horseshoe" fold and a linear conformer. The latter is exclusively found in monomeric form in solution whereas the horseshoe fold is stable in solid phase and in fibrous assemblies. Small oligomers were absent. Thus the self assembly of Ac-beta(3)[LIA] is arrested by the activation energy need of the conformation change; fibre growth might be triggered by conditions that allow increased conformational freedom of the monomers. This observation may be used to develop strategies for controlled switchable self-assembly.

  • 6.
    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 universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, 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 universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, 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 Solution2024Ingår i: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 96, nr 7, s. 3017-3024Artikel i tidskrift (Refereegranskat)
    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.

  • 7.
    Del Giudice, Rita
    et al.
    Malmö universitet, Biofilms Research Center for Biointerfaces. Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Plant Biochemistry, Department of Plant and Environmental Sciences, University of Copenhagen, Thorvaldsensvej 40, Copenhagen, DK-1871, Denmark.
    Paracini, Nicolò
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Laursen, Tomas
    Plant Biochemistry, Department of Plant and Environmental Sciences, University of Copenhagen, Thorvaldsensvej 40, DK-1871 Copenhagen, Denmark.
    Blanchet, Clement
    European Molecular Biology Laboratory (EMBL) Hamburg Outstation, DESY, 22607 Hamburg, Germany.
    Roosen-Runge, Felix
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Cárdenas, Marité
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces. Department of Biological Sciences, Nanyang Technological University, Singapore, 639798, Singapore; Biofisika Institute (CSIC, UPV/EHU), Leioa, 48940, Spain.
    Expanding the Toolbox for Bicelle-Forming Surfactant–Lipid Mixtures2022Ingår i: Molecules, ISSN 1431-5157, E-ISSN 1420-3049, Vol. 27, nr 21, s. 7628-7628Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Bicelles are disk-shaped models of cellular membranes used to study lipid–protein interactions, as well as for structural and functional studies on transmembrane proteins. One challenge for the incorporation of transmembrane proteins in bicelles is the limited range of detergent and lipid combinations available for the successful reconstitution of proteins in model membranes. This is important, as the function and stability of transmembrane proteins are very closely linked to the detergents used for their purification and to the lipids that the proteins are embedded in. Here, we expand the toolkit of lipid and detergent combinations that allow the formation of stable bicelles. We use a combination of dynamic light scattering, small-angle X-ray scattering and cryogenic electron microscopy to perform a systematic sample characterization, thus providing a set of conditions under which bicelles can be successfully formed.

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  • 8.
    Engstedt, Jenni
    et al.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces. Camurus AB, Ideon Science Park, Lund SE-223 70, Sweden.
    In 't Zandt, René
    Lund University Bioimaging Center, Lund University, Lund SE-221 84, Sweden.
    Barauskas, Justas
    Camurus AB, Ideon Science Park, Lund SE-223 70, Sweden.
    Kocherbitov, Vitaly
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Swelling kinetics of mixtures of soybean phosphatidylcholine and glycerol dioleate2024Ingår i: Colloids and Surfaces B: Biointerfaces, ISSN 0927-7765, E-ISSN 1873-4367, Vol. 239, artikel-id 113955Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Lipid-based drug delivery systems offer the potential to enhance bioavailability, reduce dosing frequency, and improve patient adherence. In aqueous environment, initially dry lipid depots take up water and form liquid crystalline phases. Variation of lipid composition, depot size and hydration-induced phase transitions will plausibly affect the diffusion in and out of the depot. Lipid depots of soybean phosphatidylcholine (SPC) and glycerol dioleate (GDO) mixtures were hydrated for varying time durations in a phosphate-buffered saline (PBS) buffer and then analyzed with Karl Fischer titration, magnetic resonance imaging (MRI) and gravimetrically. Mathematical modeling of the swelling process using diffusion equations, was used to estimate the parameters of diffusion. Both composition of lipid mixture and depot size affect swelling kinetics… The diffusion parameters obtained in Karl Fischer titration and MRI (with temporal and spatial resolution respectively) are in good agreement. Remarkably, the MRI results show a gradient of water content within the depot even after the end of diffusion process. Apparently contradicting the first Fick's law in its classical form, these results find an explanation using the generalized Fick's law that considers the gradient of chemical potential rather than concentration as the driving force of diffusion.

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  • 9.
    Filekovic, Edina
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Antioxidativ kapacitet i växtextrakt från Rhodiola rosea L, Plantago major L och Silybum marianum L2021Självständigt arbete på grundnivå (högskoleexamen), 10 poäng / 15 hpStudentuppsats (Examensarbete)
  • 10.
    Garvey, Christopher J.
    et al.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces. Laboratoire de Physique des Solides, UMR 8502, CNRS, Université Paris Saclay, 91400 Orsay, France; Lund Institute for Advanced Neutron and X-ray Science, 223 70 Lund, Sweden; Australian Nuclear Science and Technology Organisation, Locked Bag 2001, Kirrawee DC, NSW 2232, Australia.
    Impéror-Clerc, Marianne
    Laboratoire de Physique des Solides, UMR 8502, CNRS, Université Paris Saclay, 91400 Orsay, France.
    Rouzière, Stéphan
    Laboratoire de Physique des Solides, UMR 8502, CNRS, Université Paris Saclay, 91400 Orsay, France.
    Gouadec, Gwenaël
    Laboratoire MONARIS, Sorbonne Université, CNRS, c49, 75252 Paris, France.
    Boyron, Olivier
    C2P2-LCPP Group, UMR CNRS 5265, Université de Lyon, ESCPE Lyon, Bat 308F, 43 Bd du 11 novembre 1918, 69616 Villeurbanne, France.
    Rowenczyk, Laura
    Laboratoire des IMRCP, Université de Toulouse, CNRS UMR 5623, Université Paul Sabatier, 118, route de Narbonne, F-31062 Toulouse, Cedex 09, France.
    Mingotaud, Anne Françoise
    Laboratoire des IMRCP, Université de Toulouse, CNRS UMR 5623, Université Paul Sabatier, 118, route de Narbonne, F-31062 Toulouse, Cedex 09, France.
    Ter Halle, Alexandra
    Laboratoire des IMRCP, Université de Toulouse, CNRS UMR 5623, Université Paul Sabatier, 118, route de Narbonne, F-31062 Toulouse, Cedex 09, France.
    Molecular-Scale Understanding of the Embrittlement in Polyethylene Ocean Debris2020Ingår i: Environmental Science and Technology, ISSN 0013-936X, E-ISSN 1520-5851, Vol. 54, nr 18, s. 11173-11181Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The fate of plastic waste is a pressing issue since it forms a visible and long-lived reminder of the environmental impact of consumer habits. In this study, we examine the structural changes in the lamellar arrangements of semicrystalline polyethylene (PE) packaging waste with the aim of understanding the physical mechanisms of embrittlement in PE exposed to the marine environment. PE microplastics and macroplastics from identifiable PE packaging were collected in the Atlantic Ocean and compared to new PE boxes. Several experimental techniques interrogate the effects of environmental exposure on their bulk and surface properties. Size exclusion chromatography determines the molecular weight distribution of the PE polymer chains and differential scanning calorimetry gives the crystallinity. Small- and wide-angle X-ray scattering examines the packing of PE chains into semicrystalline lamellae. Longitudinal acoustic mode Raman spectroscopy provides a complementary measurement of the length of PE polymer chains extending through the crystalline lamellar domains. While there is a high degree of uncertainty in the time scale for the changes, the overall picture at the molecular scale is that although PE becomes more crystalline with environmental exposure, the lamellar order present in new packing boxes is disrupted by the weathering process. This process has important implications for embrittlement and subsequent degradation.

  • 11.
    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 universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, 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 universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, 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.2020Ingår i: Polymers, E-ISSN 2073-4360, Vol. 13, nr 1, artikel-id E120Artikel i tidskrift (Refereegranskat)
    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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  • 12.
    Hasterok, Sylwia
    et al.
    Faculty of Biology and Environmental Protection, University of Silesia, Katowice, Poland .
    Nyesiga, Barnabas
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Gjörloff Wingren, Anette
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    CD81 (Cluster of Differentiation 81)2020Ingår i: Atlas of Genetics and Cytogenetics in Oncology and Haematology, E-ISSN 1768-3262, nr 7Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    Cluster of differentiation (CD81) is a type of protein, which is encoded by CD81 gene. Beside that CD81 is also known under other names such as Target of the Antiproliferative Antibody 1 (TAPA-1) and Tetraspanin-28 (TSPAN28). Location of CD81 is known to be on chromosome 11 (11p15.5), where it contains 15-20 bases in length. It is expressed mostly in cells of testis, ovary, endometrium, placenta, bone marrow, smooth muscles and others. The main function of the CD81 protein is to mediate signal transduction events, which are important for cells' development, activation, growth and motility. The CD81 gene is also known as a candidate for many malignancies because of its location. The characteristic feature of CD81 is that it is highly hydrophobic and contains a short N- and C-terminal cytoplasmic domains together with cytoplasmic cysteines, potential sites of palmitoylation as well as four transmembrane domains where they together hold the protein in a cell membrane. There are two CD81 isoforms, isoform 1 and isoform 2. Isoforms of CD81 are usually found in a tumor-suppressor region where they have a great impact on tumor development. There has always been a high interest in research on CD81 function in viral disease development. In fact, it is known that CD81 contributes in the development of diseases such as hepatitis C, malaria and various types of cancer. Since the complete effect of CD81 is unknown, further research and scientific methodology could potentially discover all possible functions and mechanisms regulated by the CD81 protein in human body.

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  • 13.
    Hedegaard, Sofie Fogh
    et al.
    Centerfor Biopharmaceuticals and Biobarriers in Drug Delivery, Department of Pharmacy, Faculty of Health and Medical Sciences, University of Copenhagen, Universitetsparken 2, 2100 Copenhagen, Denmark.
    Bruhn, Dennis Skjøth
    PHYLIFE, Physical Life Science, Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230 Odense SØ, Denmark.
    Khandelia, Himanshu
    PHYLIFE, Physical Life Science, Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230 Odense SØ, Denmark.
    Cárdenas, Marité
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Nielsen, Hanne Mørck
    Centerfor Biopharmaceuticals and Biobarriers in Drug Delivery, Department of Pharmacy, Faculty of Health and Medical Sciences, University of Copenhagen, Universitetsparken 2, 2100 Copenhagen, Denmark.
    Shuffled lipidation pattern and degree of lipidation determines the membrane interaction behavior of a linear cationic membrane-active peptide.2020Ingår i: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 578, s. 584-597, artikel-id S0021-9797(20)30740-2Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    HYPOTHESIS: Permeation of macromolecular drugs across biological plasma membranes is a major challenge in drug delivery. Cationic cell-penetrating peptides (CPPs) are attractive functional excipient candidates for the delivery of macromolecules across membrane barriers, due to their membrane translocating ability. The properties of CPPs can be tailored by lipidation, a promising approach to facilitate enhanced membrane insertion, potentially promoting increased translocation of the CPP and cargo.

    EXPERIMENTS: To explore the impact that site and degree of lipidation have on the membrane interaction of a cationic CPP, we designed and investigated CPP conjugates with one or two fatty acid chains.

    FINDINGS: Compared to the parent CPP and the single-lipidated conjugates, the double-lipidated conjugate exhibited the most pronounced membrane perturbation effects, as measured by several biophysical techniques. The experimental findings were supported by molecular dynamics (MD) simulations, demonstrating that all CPP conjugates interacted with the membrane by insertion of the lipid chain(s) into the core of the bilayer. Moreover, membrane-thinning effects and induced membrane curvature were displayed upon CPP interaction. Our results demonstrate that the impact exerted by the CPP on the membrane is notably affected by positioning and especially the degree of lipidation, which might influence the properties of CPPs as functional excipients.

  • 14.
    Hendus-Altenburger, Ruth
    et al.
    Structural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200, Copenhagen N, Denmark; Cell Biology and Physiology, Department of Biology, University of Copenhagen, Universitetsparken 13, DK-2100, Copenhagen Ø, Denmark.
    Vogensen, Jens
    Cell Biology and Physiology, Department of Biology, University of Copenhagen, Universitetsparken 13, DK-2100, Copenhagen Ø, Denmark.
    Pedersen, Emilie Skotte
    Structural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200, Copenhagen N, Denmark.
    Luchini, Alessandra
    Niels Bohr Institute, University of Copenhagen, Universitetsparken 5, 2100, Copenhagen Ø, Denmark.
    Araya-Secchi, Raul
    Niels Bohr Institute, University of Copenhagen, Universitetsparken 5, 2100, Copenhagen Ø, Denmark.
    Bendsoe, Anne H
    Structural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200, Copenhagen N, Denmark; Cell Biology and Physiology, Department of Biology, University of Copenhagen, Universitetsparken 13, DK-2100, Copenhagen Ø, Denmark.
    Prasad, Nanditha Shyam
    Cell Biology and Physiology, Department of Biology, University of Copenhagen, Universitetsparken 13, DK-2100, Copenhagen Ø, Denmark.
    Prestel, Andreas
    Structural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200, Copenhagen N, Denmark.
    Cardenas, Marité
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Pedraz-Cuesta, Elena
    Cell Biology and Physiology, Department of Biology, University of Copenhagen, Universitetsparken 13, DK-2100, Copenhagen Ø, Denmark.
    Arleth, Lise
    Niels Bohr Institute, University of Copenhagen, Universitetsparken 5, 2100, Copenhagen Ø, Denmark.
    Pedersen, Stine F
    Cell Biology and Physiology, Department of Biology, University of Copenhagen, Universitetsparken 13, DK-2100, Copenhagen Ø, Denmark.
    Kragelund, Birthe B
    Structural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200, Copenhagen N, Denmark.
    The intracellular lipid-binding domain of human Na+/H+ exchanger 1 forms a lipid-protein co-structure essential for activity2020Ingår i: Communications Biology, E-ISSN 2399-3642, Vol. 3, nr 1, artikel-id 731Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Dynamic interactions of proteins with lipid membranes are essential regulatory events in biology, but remain rudimentarily understood and particularly overlooked in membrane proteins. The ubiquitously expressed membrane protein Na+/H+-exchanger 1 (NHE1) regulates intracellular pH (pHi) with dysregulation linked to e.g. cancer and cardiovascular diseases. NHE1 has a long, regulatory cytosolic domain carrying a membrane-proximal region described as a lipid-interacting domain (LID), yet, the LID structure and underlying molecular mechanisms are unknown. Here we decompose these, combining structural and biophysical methods, molecular dynamics simulations, cellular biotinylation- and immunofluorescence analysis and exchanger activity assays. We find that the NHE1-LID is intrinsically disordered and, in presence of membrane mimetics, forms a helical αα-hairpin co-structure with the membrane, anchoring the regulatory domain vis-a-vis the transport domain. This co-structure is fundamental for NHE1 activity, as its disintegration reduced steady-state pHi and the rate of pHi recovery after acid loading. We propose that regulatory lipid-protein co-structures may play equally important roles in other membrane proteins.

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  • 15.
    Huynh, Chau Minh
    et al.
    Department of Chemistry, Umeå University, S-90187 Umeå, Sweden.
    Mavliutova, Liliia
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Sparrman, Tobias
    Department of Chemistry, Umeå University, S-90187 Umeå, Sweden.
    Sellergren, Börje
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, 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.2023Ingår i: ACS Omega, E-ISSN 2470-1343, Vol. 8, nr 46, s. 44238-44249Artikel i tidskrift (Refereegranskat)
    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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  • 16.
    Jakubauskas, Dainius
    et al.
    Univ Copenhagen, Niels Bohr Inst, DK-2100 Copenhagen, Denmark.;Univ Copenhagen, Copenhagen Plant Sci Ctr, Dept Plant & Environm Sci, DK-1871 Copenhagen, Denmark..
    Kowalewska, Lucja
    Univ Warsaw, Fac Biol, Inst Expt Plant Biol & Biotechnol, Dept Plant Anat & Cytol, Warsaw, Poland..
    Sokolova, Anna, V
    ANSTO, Australian Ctr Neutron Scattering, Sydney, NSW 2234, Australia..
    Garvey, Christopher J.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces. ANSTO, Australian Ctr Neutron Scattering, Sydney, NSW 2234, Australia.;Lund Inst Adv Neutron & Xray Scattering, Lund, Sweden..
    Mortensen, Kell
    Univ Copenhagen, Niels Bohr Inst, DK-2100 Copenhagen, Denmark..
    Jensen, Poul Erik
    Univ Copenhagen, Copenhagen Plant Sci Ctr, Dept Plant & Environm Sci, DK-1871 Copenhagen, Denmark..
    Kirkensgaard, Jacob J. K.
    Univ Copenhagen, Niels Bohr Inst, DK-2100 Copenhagen, Denmark.;Univ Copenhagen, Dept Food Sci, DK-1871 Copenhagen, Denmark..
    Ultrastructural modeling of small angle scattering from photosynthetic membranes2019Ingår i: Scientific Reports, E-ISSN 2045-2322, Vol. 9, artikel-id 19405Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The last decade has seen a range of studies using non-invasive neutron and X-ray techniques to probe the ultrastructure of a variety of photosynthetic membrane systems. A common denominator in this work is the lack of an explicitly formulated underlying structural model, ultimately leading to ambiguity in the data interpretation. Here we formulate and implement a full mathematical model of the scattering from a stacked double bilayer membrane system taking instrumental resolution and polydispersity into account. We validate our model by direct simulation of scattering patterns from 3D structural models. Most importantly, we demonstrate that the full scattering curves from three structurally typical cyanobacterial thylakoid membrane systems measured in vivo can all be described within this framework. The model provides realistic estimates of key structural parameters in the thylakoid membrane, in particular the overall stacking distance and how this is divided between membranes, lumen and cytoplasmic liquid. Finally, from fitted scattering length densities it becomes clear that the protein content in the inner lumen has to be lower than in the outer cytoplasmic liquid and we extract the first quantitative measure of the luminal protein content in a living cyanobacteria.

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  • 17.
    Jarrett, K. J.
    et al.
    Physics and Astronomy, Curtin University, Kent Street, Bentley, 6102, WA, Australia; Australian Centre for Neutron Scattering, Australian Nuclear Science and Technology Organisation, PMB 1, Menai, 2234, NSW, Australia.
    Kirby, N.
    Australian Synchrotron, Australian Nuclear Science and Technology Organisation, Clayton, 3168, VIC, Australia.
    Buckley, C. E.
    Physics and Astronomy, Curtin University, Kent Street, Bentley, 6102, WA, Australia.
    Garvey, Christopher J.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces. Australian Centre for Neutron Scattering, Australian Nuclear Science and Technology Organisation, PMB 1, Menai, 2234, NSW, Australia; Lund Institute for Advanced Neutron and X-ray Scattering, IDEON Building: Delta 5, Scheelevägen 19, Lund, 22370, Sweden.
    The spatial modulation of microfibril angle in the woody tissue of maturing tree stems studied with synchrotron radiation2020Ingår i: Australian Journal of Botany, ISSN 0067-1924, E-ISSN 1444-9862, Vol. 68, nr 4, s. 267-274Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Spatial variations in the microfibril angle (MFA) of cellulose are mapped on individual radial sections of wood from the maturing stems of Australian tree species (Acacia floribunda, Acacia suaveolens, Acacia doratoxylon, Acacia havilandiorum, Brachychiton populneus and Bertya cunninghamii) from different rainfall and soil nutrient availabilities using synchrotron wide angle X-ray scattering. For the three species with the smallest radial variation there is a clear linear relationship between the MFA with Young's modulus and wood density with data published previously for these samples. The other three samples show a large radially symmetric variation in MFA across the radial section either having a continuous change from large MFA in the stem's centre to small value close to the bark or the reverse, small MFA at the centre to larger values close to the bark. For these samples, a strong linear correlation between the Young's modulus and density and the MFA is not apparent. We conclude that spatially localised measurements of MFA provide an important insight in the adaptation of wood tissue to environmental conditions.

  • 18.
    Kimani, Martha
    et al.
    Bundesanstalt Mat Forsch & Prufung BAM, Chem & Opt Sensing Div 1 9, D-12489 Berlin, Germany..
    Beyer, Sarah
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    El-Schich, Zahra
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Gawlitza, Kornelia
    Bundesanstalt Mat Forsch & Prufung BAM, Chem & Opt Sensing Div 1 9, D-12489 Berlin, Germany..
    Gjörloff-Wingren, Anette
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Rurack, Knut
    Bundesanstalt Mat Forsch & Prufung BAM, Chem & Opt Sensing Div 1 9, D-12489 Berlin, Germany..
    Imprinted Particles for Direct Fluorescence Detection of Sialic Acid in Polar Media and on Cancer Cells with Enhanced Control of Nonspecific Binding2021Ingår i: ACS APPLIED POLYMER MATERIALS, ISSN 2637-6105, Vol. 3, nr 5, s. 2363-2373Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Glycoproteins are abundant on the cell surface of mammals, providing structural support, modulating cell membrane properties, and acting as signaling agents. Variation of glycosylation patterns has been found to indicate various disease states, including cell malignancy. Sialic acid (SA) is present as a terminating group on cell-surface glycans, and its overexpression has been linked to several types of cancer. Detection of SA on the cell surface is therefore critical for detection of cancer in its early stages. In this work, a fluorescent molecularly imprinted polymer layer targeting SA was synthesized on the surface of silica-coated polystyrene (PS) particles. Compared to previous works, a PS core supplies a lighter, lower-density support for improved suspension stability and scattering properties. Moreover, their smaller size provides a higher surface-area-to-volume ratio for binding. The incorporation of a fluorescent monomer in the MIP shell allowed for simple and rapid determination of binding specificity in polar media due to a deprotonation-reprotonation interaction mechanism between the fluorescent monomer and SA, which led to spectral changes. Upon titration of the MIP particles with SA in suspension, an increase in fluorescence emission of the particles was observed, with the MIP particles binding SA more selectively compared to the nonimprinted polymer (NIP) control particles. In cell staining experiments performed by flow cytometry, the binding behavior of the MIP particles compared favorably with that of SA-binding lectins. NIPs prepared with a "dummy" template served as a better negative control in cell binding assays due to the favorable inward orientation of template-binding functional groups in the polymer shell, which reduced nonspecific binding. The results show that fluorescent MIPs targeting SA are a promising tool for in vitro fluorescence staining of cancerous cells and for future diagnosis of cancer at early stages.

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  • 19.
    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 universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (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 universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, 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.2023Ingår i: Journal of materials chemistry. B, ISSN 2050-750X, E-ISSN 2050-7518, Vol. 11, nr 45, s. 10873-10882Artikel i tidskrift (Refereegranskat)
    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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  • 20.
    Leo, Fredrik
    et al.
    Malmö universitet, Odontologiska fakulteten (OD). Malmö universitet, Biofilms Research Center for Biointerfaces. Genovis AB, Lund, Sweden..
    Svensäter, Gunnel
    Malmö universitet, Odontologiska fakulteten (OD). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Lood, Rolf
    Lund Univ, Fac Med, Dept Clin Sci Lund, Div Infect Med, Lund, Sweden..
    Wickström, Claes
    Malmö universitet, Odontologiska fakulteten (OD). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Characterization of a highly conserved MUC5B-degrading protease, MdpL, from Limosilactobacillus fermentum2023Ingår i: Frontiers in Microbiology, E-ISSN 1664-302X, Vol. 14, artikel-id 1127466Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    MUC5B is the predominant glycoprotein in saliva and is instrumental in the establishment and maintenance of multi-species eubiotic biofilms in the oral cavity. Investigations of the aciduric Lactobacillaceae family, and its role in biofilms emphasizes the diversity across different genera of the proteolytic systems involved in the nutritional utilization of mucins. We have characterized a protease from Limosilactobacillus fermentum, MdpL (Mucin degrading protease from Limosilactobacillus) with a high protein backbone similarity with commensals that exploit mucins for attachment and nutrition. MdpL was shown to be associated with the bacterial cell surface, in close proximity to MUC5B, which was sequentially degraded into low molecular weight fragments. Mapping the substrate preference revealed multiple hydrolytic sites of proteins with a high O-glycan occurrence, although hydrolysis was not dependent on the presence of O-glycans. However, since proteolysis of immunoglobulins was absent, and general protease activity was low, a preference for glycoproteins similar to MUC5B in terms of glycosylation and structure is suggested. MdpL preferentially hydrolyzed C-terminally located hydrophobic residues in peptides larger than 20 amino acids, which hinted at a limited sequence preference. To secure proper enzyme folding and optimal conditions for activity, L. fermentum incorporates a complex system that establishes a reducing environment. The importance of overall reducing conditions was confirmed by the activity boosting effect of the added reducing agents L-cysteine and DTT. High activity was retained in low to neutral pH 5.5-7.0, but the enzyme was completely inhibited in the presence of Zn2+. Here we have characterized a highly conserved mucin degrading protease from L. fermentum. MdpL, that together with the recently discovered O-glycanase and O-glycoprotease enzyme groups, increases our understanding of mucin degradation and complex biofilm dynamics.

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  • 21.
    Luchini, Alessandra
    et al.
    European Spallat Source ERIC, Partikelgatan, S-22484 Lund, Sweden.;Univ Perugia, Dept Phys & Geol, I-06123 Perugia, Italy..
    Tidemand, Frederik Gronbaek
    Univ Copenhagen, Dept Plant & Environm Sci, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark..
    Johansen, Nicolai Tidemand
    Univ Copenhagen, Dept Plant & Environm Sci, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark..
    Sebastiani, Federica
    Malmö universitet, Biofilms Research Center for Biointerfaces. Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Corucci, Giacomo
    Inst Laue Langevin, 71 Ave Martyrs,BP 156, F-38042 Grenoble, France.;Univ Grenoble Alpes, Ecole Doctorale Phys, 110 Rue Chim, F-38400 St Martin Dheres, France..
    Fragneto, Giovanna
    Inst Laue Langevin, 71 Ave Martyrs,BP 156, F-38042 Grenoble, France.;Univ Grenoble Alpes, Ecole Doctorale Phys, 110 Rue Chim, F-38400 St Martin Dheres, France..
    Cárdenas, Marité
    Malmö universitet, Biofilms Research Center for Biointerfaces. Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Arleth, Lise
    Univ Copenhagen, Niels Bohr Inst, Univ Parken 5, DK-2100 Copenhagen, Denmark..
    Dark peptide discs for the investigation of membrane proteins in supported lipid bilayers: the case of synaptobrevin 2 (VAMP2)2022Ingår i: Nanoscale Advances, E-ISSN 2516-0230, Vol. 10, nr 17Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Supported lipid bilayers (SLBs) are commonly used as model systems mimicking biological membranes. Recently, we reported a new method to produce SLBs with incorporated membrane proteins, which is based on the application of peptide discs [Luchini et al., Analytical Chemistry, 2020, 92, 1081-1088]. Peptide discs are small discoidal particles composed of a lipid core and an outer belt of self-assembled 18A peptides. SLBs including membrane proteins can be formed by depositing the peptide discs on a solid support and subsequently removing the peptide by buffer rinsing. Here, we introduce a new variant of the 18A peptide, named dark peptide (d18A). d18A exhibits UV absorption at 214 nm, whereas the absorption at 280 nm is negligible. This improves sample preparation as it enables a direct quantification of the membrane protein concentration in the peptide discs by measuring UV absorption at 280 nm. We describe the application of the peptide discs prepared with d18A (dark peptide discs) to produce SLBs with a membrane protein, synaptobrevin 2 (VAMP2). The collected data showed the successful formation of SLBs with high surface coverage and incorporation of VAMP2 in a single orientation with the extramembrane domain exposed towards the bulk solvent. Compared to 18A, we found that d18A was more efficiently removed from the SLB. Our data confirmed the structural organisation of VAMP2 as including both alpha-helical and beta-sheet secondary structure. We further verified the orientation of VAMP2 in the SLBs by characterising the binding of VAMP2 with alpha-synuclein. These results point at the produced SLBs as relevant membrane models for biophysical studies as well as nanostructured biomaterials.

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  • 22.
    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 universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, 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 Mimics2022Ingår i: International Journal of Molecular Sciences, ISSN 1661-6596, E-ISSN 1422-0067, Vol. 23, nr 5, artikel-id 2534Artikel i tidskrift (Refereegranskat)
    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.

  • 23.
    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 polymers2021Ingår i: RSC Advances, E-ISSN 2046-2069, Vol. 11, nr 36, s. 22409-22418Artikel i tidskrift (Refereegranskat)
    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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  • 24.
    Mavliutova, Liliia
    et al.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Verduci, Elena
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Shinde, Sudhirkumar
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Sellergren, Börje
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Combinatorial Design of a Sialic Acid-Imprinted Binding Site2021Ingår i: ACS Omega, E-ISSN 2470-1343, Vol. 6, nr 18, s. 12229-12237Artikel i tidskrift (Refereegranskat)
    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.

  • 25.
    Nielsen, Josefine
    et al.
    Univ Oslo, Dept Chem, Oslo, Norway.
    Bjørnestad, Victoria Ariel
    Univ Oslo, Dept Chem, Oslo, Norway.
    Lind, Tania Kjellerup
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Jenssen, Havard
    Roskilde Univ, Dept Sci & Environm, Roskilde, Denmark..
    Cárdenas, Marité
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Lund, Reidar
    Univ Oslo, Dept Chem, Oslo, Norway.
    Indolicidin as a model antimicrobial peptide: investigating their interactions with lipid vesicles and supported bilayers2018Ingår i: Abstracts of Papers of the American Chemical Society, ISSN 0065-7727, Vol. 255Artikel i tidskrift (Övrigt vetenskapligt)
  • 26.
    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 PEGylation2020Ingår i: RSC Advances, E-ISSN 2046-2069, Vol. 10, s. 35329-35340, artikel-id 35329Artikel i tidskrift (Refereegranskat)
    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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  • 27.
    Nielsen, Josefine Eilsø
    et al.
    Department of Chemistry, University of Oslo, 0315 Oslo, Norway.
    Lind, Tania Kjellerup
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Lone, Abdullah
    Department of Science and Environment, Roskilde University, 4000 Roskilde, Denmark.
    Gerelli, Yuri
    Institut Laue - Langevin, 38000 Grenoble, France.
    Hansen, Paul Robert
    Department of Drug Design and Pharmacology, University of Copenhagen, 2100 Copenhagen, Denmark.
    Jenssen, Håvard
    Department of Science and Environment, Roskilde University, 4000 Roskilde, Denmark.
    Cárdenas, Marité
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Lund, Reidar
    Department of Chemistry, University of Oslo, 0315 Oslo, Norway.
    A biophysical study of the interactions between the antimicrobial peptide indolicidin and lipid model systems2019Ingår i: Biochimica et Biophysica Acta - Biomembranes, ISSN 0005-2736, E-ISSN 1879-2642, Vol. 1861, nr 7, s. 1355-1364Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The naturally occurring peptide indolicidin from bovine neutrophils exhibits strong biological activity against a broad spectrum of microorganisms. This is believed to arise from selective interactions with the negatively charged cytoplasmic lipid membrane found in bacteria. We have investigated the peptide interaction with supported lipid model membranes using a combination of complementary surface sensitive techniques: neutron reflectometry (NR), atomic force microscopy (AFM), and quartz crystal microbalance with dissipation monitoring (QCM-D). The data are compared with small-angle X-ray scattering (SAXS) results obtained with lipid vesicle/peptide solutions. The peptide membrane interaction is shown to be significantly concentration dependent. At low concentrations, the peptide inserts at the outer leaflet in the interface between the headgroup and tail core. Insertion of the peptide results in a slight decrease in the lipid packing order of the bilayer, although not sufficient to cause membrane thinning. By increasing the indolicidin concentration well above the physiologically relevant conditions, a deeper penetration of the peptide into the bilayer and subsequent lipid removal take place, resulting in a slight membrane thinning. The results suggest that indolicidin induces lipid removal and that mixed indolicidin-lipid patches form on top of the supported lipid bilayers. Based on the work presented using model membranes, indolicidin seems to act through the interfacial activity model rather than through the formation of stable pores.

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  • 28.
    Nyesiga, Barnabas
    et al.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    El-Schich, Zahra
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    CD22 (CD22 molecule)2020Ingår i: Atlas of Genetics and Cytogenetics in Oncology and Haematology, E-ISSN 1768-3262, nr 12Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    Sialic acid binding immunoglobulin-type lectin (Siglec) family are inhibitory receptors with diverse roles in the immune system. Siglec family contains 14 members in human and 9 in murine. Differentially expressed on various white blood cells. Here in this review we are focusing on CD22, also known as Sialic Acid-Binding Ig-Like Lectin 2 (Siglec-2). CD22 gene is located on 19q13.12 and is encoding a 140 kD type I transmembrane glycoprotein on the surface of B cells and is part of the immunoglobulin (Ig) superfamily and has been found only on B cells. CD22 has been shown to play a major role in establishing a baseline level of B-cell inhibition, and thus is a critical determinant of homeostasis in humoral immunity.

  • 29.
    Olsson, Amanda
    Malmö universitet, Fakulteten för hälsa och samhälle (HS).
    Utvärdering av fem olika metoder för DNA-extraktion från bakterier2023Självständigt arbete på grundnivå (kandidatexamen), 10 poäng / 15 hpStudentuppsats (Examensarbete)
    Abstract [sv]

    På huden lever en sammansättning av olika mikroorganismer såsom bakterier, svampar och virus. Dessa mikroorganismer kallas hudens mikrobiom. Sammansättningen av en individs mikrobiom kan ge mycket information om en individens hälsa. För att undersöka sammansättningen av bakterier på hudytan med exempelvis qPCR, behöver bakterier samlas in och DNA extraheras. Bakteriekoncentrationen på hudens torrare områden som exempelvis armar har normalt en relativt låg bakteriekoncentration vid 102-104 bakterier per cm2. Huden koloniseras till stor del av grampositiva bakterier. Grampositiva bakterier är i regel svårare att lysera än andra bakterier och kräver därför hårdare lysering. En bra extraktionsmetod ska erhålla mycket DNA utan att påverka dess kvalité. I detta arbete utvärderades initialt fem olika extraktionsmetoder på bakteriesuspension med Staphylococcus aureus (S. aureus), både direkt på bakteriesuspension men också från svabb. Utvärdering gjordes på PureLink Microbiome DNA Purification Kit, QlAamp PowerFecal Pro, QlAamp DNA Mini Kit och KOH-EDTA. Metoden med QlAamp DNA Mini Kit testades med två olika protokoll och räknades som två separata metoder. Metoderna som gav bäst resultat vid initial utvärdering var PureLink Microbiome och KOH-EDTA. Därefter utvärderades dessa två metoderna på prov insamlat med svabb från huden på 10 frivilliga deltagare. 

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  • 30.
    Paracini, Nicolò
    et al.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Clifton, Luke A
    ISIS Pulsed Neutron and Muon Source, Rutherford Appleton Laboratory, Harwell Oxford, Didcot OX11 0QX, U.K.
    Lakey, Jeremy H
    Biosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne NE2 4HH, U.K.
    Studying the surfaces of bacteria using neutron scattering: finding new openings for antibiotics.2020Ingår i: Biochemical Society Transactions, ISSN 0300-5127, E-ISSN 1470-8752, Vol. 48, nr 5, s. 2139-2149, artikel-id BST20200320Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The use of neutrons as a scattering probe to investigate biological membranes has steadily grown in the past three decades, shedding light on the structure and behaviour of this ubiquitous and fundamental biological barrier. Meanwhile, the rise of antibiotic resistance has catalysed a renewed interest in understanding the mechanisms underlying the dynamics of antibiotics interaction with the bacterial cell envelope. It is widely recognised that the key reason behind the remarkable success of Gram-negative pathogens in developing antibiotic resistance lies in the effectiveness of their outer membrane (OM) in defending the cell from antibacterial compounds. Critical to its function, the highly asymmetric lipid distribution between the inner and outer bilayer leaflets of the OM, adds an extra level of complexity to the study of this crucial defence barrier. Here we review the opportunities offered by neutron scattering techniques, in particular reflectometry, to provide structural information on the interactions of antimicrobials with in vitro models of the OM. The differential sensitivity of neutrons towards hydrogen and deuterium makes them a unique probe to study the structure and behaviour of asymmetric membranes. Molecular-level understanding of the interactions between antimicrobials and the Gram-negative OM provides valuable insights that can aid drug development and broaden our knowledge of this critically important biological barrier.

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  • 31.
    Phan-Xuan, Tuan
    et al.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces. Max IV Laboratory, Lund University, 224 84 Lund, Sweden.
    Bogdanova, Ekaterina
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Millqvist Fureby, Anna
    RISE Research Institutes of Sweden, 114 86 Stockholm, Sweden.
    Fransson, Jonas
    SOBI Swedish Orphan Biovitrum, 112 76 Stockholm, Sweden.
    Terry, Ann E
    Max IV Laboratory, Lund University, 224 84 Lund, Sweden.
    Kocherbitov, Vitaly
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Hydration-Induced Structural Changes in the Solid State of Protein: A SAXS/WAXS Study on Lysozyme.2020Ingår i: Molecular Pharmaceutics, ISSN 1543-8384, E-ISSN 1543-8392, Vol. 17, nr 9, s. 3246-3258Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The stability of biologically produced pharmaceuticals is the limiting factor to various applications, which can be improved by formulation in solid-state forms, mostly via lyophilization. Knowledge about the protein structure at the molecular level in the solid state and its transition upon rehydration is however scarce, and yet it most likely affects the physical and chemical stability of the biological drug. In this work, synchrotron small- and wide-angle X-ray scattering (SWAXS) are used to characterize the structure of a model protein, lysozyme, in the solid state and its structural transition upon rehydration to the liquid state. The results show that the protein undergoes distortion upon drying to adopt structures that can continuously fill the space to remove the protein-air interface that may be formed upon dehydration. Above a hydration threshold of 35 wt %, the native structure of the protein is recovered. The evolution of SWAXS peaks as a function of water content in a broad range of concentrations is discussed in relation to the structural changes in the protein. The findings presented here can be used for the design and optimization of solid-state formulations of proteins with improved stability.

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  • 32.
    Ramonas, E.
    et al.
    Faculty of Fundamental Sciences, Vilnius Gediminas Technical University, Saulėtekio al. 11, LT-10223 Vilnius, Lithuania; Institute of Biochemistry, Life Sciences Center, Vilnius University, Saulėtekio al. 7, LT-10257 Vilnius, Lithuania.
    Shafaat, Atefeh
    Malmö universitet, Biofilms Research Center for Biointerfaces. Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Dagys, M.
    Institute of Biochemistry, Life Sciences Center, Vilnius University, Saulėtekio al. 7, LT-10257 Vilnius, Lithuania.
    Ruzgas, Tautgirdas
    Malmö universitet, Biofilms Research Center for Biointerfaces. Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Ratautas, D.
    Faculty of Fundamental Sciences, Vilnius Gediminas Technical University, Saulėtekio al. 11, LT-10223 Vilnius, Lithuania; Institute of Biochemistry, Life Sciences Center, Vilnius University, Saulėtekio al. 7, LT-10257 Vilnius, Lithuania.
    Revising catalytic “acceleration” of enzymes on citrate-capped gold nanoparticles2021Ingår i: Journal of Catalysis, ISSN 0021-9517, E-ISSN 1090-2694, Vol. 404, s. 570-578Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    In recent years, many papers have reported a catalytic “acceleration” of enzymes when immobilized on gold nanoparticles. Concordantly, gold nanoparticles are often considered as an inert and safe nanomaterial, and are widely used for various purposes, e.g., experiments with humans are being conducted in vivo. In this work we have carried out an in-detail study of catalytic properties of citrate-capped gold nanoparticles and gold nanoparticle-protein conjugates using three model proteins – enzymes glucose oxidase and catalase, and catalytically inactive protein bovine serum albumin. Catalytic properties were studied at different protein-nanoparticle ratios. UV–Vis, DLS, AFM and ζ potential measurements confirmed protein-nanoparticle conjugate formation. Catalytic activity measurements were conducted using oxygen electrode and the data were analyzed by modeling the activity of conjugates. The designed experiments demonstrated that gold nanoparticles form stable conjugates with all the investigated proteins, yet they do not increase catalytic activity of the investigated enzymes – in certain conditions gold nanoparticles mimic enzymatic reactions, which may be misattributed to accelerated enzymatic catalysis. Additionally, we present specific key points demonstrating why it may be difficult to differentiate between enzyme- and gold nanoparticle-catalyzed reactions, as well as suggest specific measurements enabling better differentiation. We do not claim that enzymes cannot be accelerated on nanoparticles in general, but rather emphasize, that experimental results demonstrating atypical catalytic performance of enzymes on nanoparticles should be interpreted with additional care, and a widely propagated view of “inert gold nanoparticles” should probably be reconsidered. 

  • 33.
    Robertsson, Carolina
    Malmö universitet, Odontologiska fakulteten (OD). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Responses to External Cues in Oral Bacteria2023Doktorsavhandling, sammanläggning (Övrigt vetenskapligt)
    Abstract [sv]

    Avhandlingen undersöker orala bakteriers svar till utifrån kommande signaler på en molekylärbiologisk nivå. I delarbete I kartläggs proteiner med serin/treonin/ tyrosin fosforylering i relation till det generella proteomet hos en oral streptokock (Streptococcus gordonii DL1). De identifierade fosfoproteinerna kunde kopplas till olika bakteriella processer, varav flera av intresse ur kariessynpunkt. Jämförelse mot andra bakteriers fosfoproteom visade många likheter, vilket är av intresse för identifiering av delade fosforyleringsprofiler. 

    I delarbete II undersöks skillnader i det generella proteomet hos S. gordonii DL1 mellan tillväxtfaserna planktonisk och biofilm, samt reglerande effekter av salivmucinet MUC5B på biofilmscellerna proteinuttryck. Skillnaderna i proteinuttryck mellan tillväxtfaser ger ledtrådar om bakteriernas mekanismer för anpassning till biofilmstillväxt. 

    Delarbete III studeras salivmucinet MUC5Bs reglerande roll på vidhäftning och metabolism i biofilmer med kliniska isolat av S. gordonii CW samt Actinomyces naeslundii CW. S. gordonii ökade vidhäftningen av A. naeslundii till MUC5B. Båda arterna kunde också använda MUC5B som enda näringskälla under tidig biofilmsbildning, både enskilt och tillsammans. Responserna som MUC5B framkallade i biofilmerna (paper II och III) verkar främja kolonisering av kommensaler och samtidigt nedreglera kariesrelaterade aktiviteter. 

    Mikrobiologiska studier fokuserar ofta på dysbiosis och sjukdomsutveckling, men mekanismer som bibehåller eubiosis är minst lika viktiga för att förstå hur oral hälsa kan främjas. Resultat kopplade till orala bakteriers svar på utifrån kommande signaler kan bidra till framtida utveckling av nya strategier för prevention och identifiering av prediktiva biomarkörer för oral hälsa. 

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  • 34.
    Rouhi, Mona
    et al.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmo Univ, Fac Hlth & Soc, Dept Biomed Sci, SE-20506 Malmo, Sweden..
    Incel, Anil
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Shinde, Sudhirkumar
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces. World Peace Univ, Sch Consciousness, Dr Vishwanath Karad Maharashtra Inst Technol, Pune 411038, Maharashtra, India..
    Role of Comonomers in the Recognition of Anionic Biomolecules in Water: Hydrogen-Bonded Imprinted Polymeric Receptor2021Ingår i: ACS APPLIED POLYMER MATERIALS, ISSN 2637-6105, Vol. 3, nr 10, s. 4904-4912Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The field of anion recognition in aqueous media is dominated by multiple positive charges and/or metal ions containing synthetic receptors. Here, we report the synthesis of a highly water-compatible oxyanion-imprinted neutral receptor by cross-linking the polymerizable diary! urea host monomer and phenyl phosphonic acid (PPA) complex in the presence of a large number of comonomers containing hydroxyl or methyl ester groups. We have demonstrated that the affinity of the imprinted receptor for anions is easily tuned by decorating the hydrophilic and hydrophobic end groups around the binding pocket of the imprinted receptor. The binding characteristics of the synthesized artificial binders were evaluated in aqueous and nonaqueous environments. We have demonstrated practical applicability of the PPA-imprinted receptor by packing in the solid-phase extraction cartridge which was used to separate the ubiquitous pesticide glyphosate from water. Also, the developed receptor can selectively bind to phosphorylated tyrosine amino acids and phosphorylated tyrosine octapeptides in aqueous buffered media than to other phosphorylated and nonphosphorylated analogues. The approach utilized here to use an inexpensive dummy template can be utilized for the synthesis of imprinted receptors for anions with phosphate motifs.

  • 35.
    Sebastiani, Federica
    et al.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Yanez Arteta, Marianna
    Advanced Drug Delivery, Pharmaceutical Sciences, R&D, AstraZeneca, Gothenburg, Sweden.
    Lindfors, Lennart
    Advanced Drug Delivery, Pharmaceutical Sciences, R&D, AstraZeneca, Gothenburg, Sweden.
    Cárdenas, Marité
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Screening of the binding affinity of serum proteins to lipid nanoparticles in a cell free environment2021Ingår i: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 610, s. 766-774, artikel-id S0021-9797(21)02028-2Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Lipid nanoparticles (LNPs) are promising drug and gene carriers. Upon intravenous administration, LNPs' experience different degree of cellular uptake depending on their formulation. Currently, in vitro and in vivo studies are the gold standard for assessing the fate of nano carriers once administered, but they are time consuming and expensive. In this work, we propose a time and cost-effective method to screen a wide range of LNP formulations and select the most promising candidates for in vitro and in vivo studies. Two different approaches were explored to investigate the binding affinity between LNPs and serum proteins using sensor functionalisation with either protein specific antibody or PEG specific antibody. The first approach allowed to identify the presence of a specific protein in the protein corona of lipid particles (reconstituted and native high-density lipoproteins (rHDL and HDL), and low-density lipoproteins LDL); while the second one provided a versatile platform for the immobilisation of pegylated-particles in order to follow the interaction with serum proteins and hence predict the composition of LNP protein corona. Sensing was done using Quartz Crystal Microbalance with Dissipation (QCM-D) but the approach is extendable to other surface sensing techniques such as Surface Plasmon Resonance (SPR) or ellipsometry.

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  • 36.
    Shinde, Sudhirkumar
    et al.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces. Dr Vishwanath Karad MIT World Peace Univ, Sch Consciousness, Pune 411038, Maharashtra, India..
    Mansour, Mona
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces. Egyptian Petr Res Inst, Anal & Evaluat Dept, 1 Ahmed Zomor St, Cairo, Egypt..
    Mavliutova, Liliia
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Incel, Anil
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Wierzbicka, Celina
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Abdel-Shafy, Hussein, I
    Natl Res Ctr, Water Res & Pollut Control Dept, Cairo 11727, Egypt..
    Sellergren, Börje
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Oxoanion Imprinting Combining Cationic and Urea Binding Groups: A Potent Glyphosate Adsorber2022Ingår i: ACS Omega, E-ISSN 2470-1343, Vol. 7, nr 1Artikel i tidskrift (Refereegranskat)
    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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  • 37.
    Shleev, Sergey
    et al.
    Malmö högskola, Fakulteten för hälsa och samhälle (HS). Department of Analytical Chemistry, Lund University, P.O. Box 124, 221 00 Lund, Sweden; Laboratory of Chemical Enzymology, A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky Pr. 33, 119071 Moscow, Russia.
    Reimann, Curt T.
    Department of Analytical Chemistry, Lund University, P.O. Box 124, 221 00 Lund, Sweden.
    Serezhenkov, Vladimir
    N.N. Semenov Institute of Chemical Physics, Russian Academy of Sciences, Kosigina 4, 119977 Moscow, Russia.
    Burbaev, Dosymzhan
    N.N. Semenov Institute of Chemical Physics, Russian Academy of Sciences, Kosigina 4, 119977 Moscow, Russia.
    Yaropolov, Alexander I.
    Laboratory of Chemical Enzymology, A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky Pr. 33, 119071 Moscow, Russia.
    Gorton, Lo
    Department of Analytical Chemistry, Lund University, P.O. Box 124, 221 00 Lund, Sweden.
    Ruzgas, Tautgirdas
    Malmö högskola, Fakulteten för hälsa och samhälle (HS).
    Autoreduction and aggregation of fungal laccase in solution phase: possible correlation with a resting form of laccase2006Ingår i: Biochimie, ISSN 0300-9084, E-ISSN 1638-6183, Vol. 88, nr 9, s. 1275-1285Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    This paper reports results of a reexamination of some poorly understood peculiarities of laccases, an enzyme family which has been extensively studied in our laboratories as well as by others for some years. The issue that is reconsidered here is the previously proposed existence of “active” and “resting” forms of laccases. The presence of fungal laccases with partly reduced active sites is demonstrated. Of further interest is that an aggregated state in solution, not to our knowledge previously noted for laccase, has been found by using small-angle X-ray scattering as well as thorough analysis of the results of several biochemical experiments. Under some conditions, this aggregated state may correlate with the resting form of the laccases, although this resting form could have a broader significance. It was shown that Trametes ochracea laccase had some anomalous characteristics, which could be correlated with the high concentration of the “resting” enzyme. The mechanism of formation of resting laccase is suggested. Knowledge of the resting state is of importance for in vitro studies. Additionally, a suggestion about the possible regulatory role of this form in vivo is mentioned.

  • 38.
    Sun, Lingbo
    et al.
    Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine and School of Dentistry, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark.
    Konstantinidi, Andriana
    Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine and School of Dentistry, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark.
    Ye, Zilu
    Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine and School of Dentistry, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark.
    Nason, Rebecca
    Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine and School of Dentistry, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark.
    Zhang, Yuecheng
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Büll, Christian
    Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine and School of Dentistry, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark.
    Kahl-Knutson, Barbro
    Department of Laboratory Medicine, Section MIG, Lund University BMC-C1228b, Klinikgatan28, 221 84 Lund, Sweden.
    Hansen, Lars
    Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine and School of Dentistry, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark.
    Leffler, Hakon
    Department of Laboratory Medicine, Section MIG, Lund University BMC-C1228b, Klinikgatan28, 221 84 Lund, Sweden.
    Vakhrushev, Sergey Y
    Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine and School of Dentistry, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark.
    Yang, Zhang
    Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine and School of Dentistry, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark.
    Clausen, Henrik
    Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine and School of Dentistry, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark.
    Narimatsu, Yoshiki
    Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine and School of Dentistry, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark.
    Installation of O-glycan sulfation capacities in human HEK293 cells for display of sulfated mucins2021Ingår i: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 298, nr 2, artikel-id 101382Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The human genome contains at least 35 genes that encode Golgi sulfotransferases that function in the secretory pathway, where they are involved in decorating glycosaminoglycans, glycolipids, and glycoproteins with sulfate groups. Although a number of important interactions by proteins such as Selectins, Galectins, and Siglecs are thought to mainly rely on sulfated O-glycans, our insight into the sulfotransferases that modify these glycoproteins, and in particular GalNAc-type O-glycoproteins, is limited. Moreover, sulfated mucins appear to accumulate in respiratory diseases, arthritis, and cancer. To explore further the genetic and biosynthetic regulation of sulfated O-glycans, here we expanded a cell-based glycan array in the human HEK293 cell line with sulfation capacities. We stably engineered O-glycan sulfation capacities in HEK293 cells by site-directed knock-in of sulfotransferase genes in combination with knockout of genes to eliminate endogenous O-glycan branching (core2 synthase gene GCNT1) and/or sialylation capacities in order to provide simplified substrates (core1 Galβ1-3GalNAcα1-O-Ser/Thr) for the introduced sulfotransferases. Expression of the galactose 3O-sulfotransferase 2 (GAL3ST2) in HEK293 cells resulted in sulfation of core1 and core2 O-glycans, whereas expression of galactose 3O-sulfotransferase 4 (GAL3ST4) resulted in sulfation of core1 only. We used the engineered cell library to dissect the binding specificity of galectin-4 and confirmed binding to the 3-O-sulfo-core1 O-glycan. This is a first step towards expanding the emerging cell-based glycan arrays with the important sulfation modification for display and production of glycoconjugates with sulfated O-glycans.

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  • 39.
    Svärd, Anna
    et al.
    Laboratory of Molecular Materials, Division of Biophysics and Bioengineering, Department of Physics, Chemistry and Biology (IFM), Linköping University, Linköping, 581 83, Sweden; Cardiovascular Research Centre (CVRC), School of Medical Sciences, Örebro University, Örebro, 70182, Sweden.
    Neilands, Jessica
    Malmö universitet, Odontologiska fakulteten (OD). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Palm, Eleonor
    Cardiovascular Research Centre (CVRC), School of Medical Sciences, Örebro University, Örebro, 70182, Sweden.
    Svensäter, Gunnel
    Malmö universitet, Odontologiska fakulteten (OD). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Bengtsson, Torbjörn
    Cardiovascular Research Centre (CVRC), School of Medical Sciences, Örebro University, Örebro, 70182, Sweden.
    Aili, Daniel
    Laboratory of Molecular Materials, Division of Biophysics and Bioengineering, Department of Physics, Chemistry and Biology (IFM), Linköping University, Linköping, 581 83, Sweden.
    Protein-Functionalized Gold Nanoparticles as Refractometric Nanoplasmonic Sensors for the Detection of Proteolytic Activity of Porphyromonas gingivalis2020Ingår i: ACS Applied Nano Materials, E-ISSN 2574-0970, Vol. 3, nr 10, s. 9822-9830Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Periodontitis is an inflammatory oral disease that affects a large part of the adult population, causing significant costs and suffering. The key pathogen, Porphyromonas gingivalis, secretes gingipains, which are highly destructive proteases and the most important virulence factors in the pathogenesis of the disease. Currently, periodontitis is diagnosed mainly by mechanical manual probing and radiography, often when the disease has already progressed significantly. The possibilities of detecting gingipain activity in gingival fluid could enable early-stage diagnosis and facilitate treatment. Here, we describe a sensitive nanoparticle-based nanoplasmonic biosensor for the detection of the proteolytic activity of gingipains. Gold nanoparticles (AuNPs) were self-assembled as a submonolayer in multiwell plates and further modified with casein or IgG. The proteolytic degradation of the protein coating was tracked by monitoring the shift in the localized surface plasmon resonance (LSPR) peak position. The sensor performance was investigated using model systems with trypsin and purified gingipains (subtypes Kgp and RgpB) and further validated using supernatants from cultures of P. gingivalis. Proteolytic degradation by proteases in buffer results in a concentration- and time-dependent blueshift of the LSPR band of about 1-2 nm when using casein as a substrate. In bacterial supernatants, the degradation of the protein coating resulted in unspecific binding of proteins present in the complex sample matrix to the nanoparticles, which instead triggered a redshift of about 2 nm of the LSPR band. A significant LSPR shift was seen only in samples with gingipain activity. The sensor showed a limit of detection < 0.1 mu g/mL (4.3 nM), which is well below gingipain concentrations detected in severe chronic periodontitis cases (similar to 50 mu g/mL). This work shows the possibility of developing cost-effective nanoparticle-based biosensors for rapid detection of protease activity for chair-side periodontal diagnostics.

  • 40.
    Waldie, Sarah
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Model Membranes and Their Interactions with Native and Artificial Lipoproteins2020Doktorsavhandling, sammanläggning (Övrigt vetenskapligt)
    Abstract [en]

    Atherosclerosis arises from build-up of plaque in the blood, can result in cardiovascular disease and is the largest killer in the west. Low- and high-density lipoproteins are involved in the disease development by depositing and removing lipids to and from artery walls. These processes are complex and not fully understood however, therefore determining the specific roles of the components involved is of fundamental importance in the treatment of the disease.

    The work presented in this thesis investigates the production of recombinant tailor-deuterated cholesterol, the structure of cholesterol-containing model membranes and interactions of both native and reconstituted lipoproteins with model membranes. Deuteration is commonly used in neutron scattering for biological samples to provide highly important contrast and the complexity of the native lipoproteins leads to the use of more simple model systems where the compositions can be altered and investigated systematically.

    A protocol was developed to produce matchout-deuterated cholesterol for use in neutron scattering studies, as cholesterol is a hugely important component in membranes. The verification of the matchpoint of cholesterol was determined by small-angle neutron scattering and the localisation of cholesterol in model membranes was determined through the use of neutron reflectometry. The interactions of the native and reconstituted lipoproteins with model membranes were also followed by neutron reflectometry, while the structural characterisation of the reconstituted lipoproteins was carried out by small-angle scattering.

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  • 41.
    Waldie, Sarah Hannah Anne
    et al.
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Browning, Kathryn
    Uppsala Univ, Dept Pharm, Uppsala, Sweden.
    Moulin, Martine
    ILL Grenoble, Life Sci Grp, Grenoble, France.
    Haertlein, Michael
    ILL Grenoble, Life Sci Grp, Grenoble, France.
    Forsyth, Trevor
    ILL Grenoble, Life Sci Grp, Grenoble, France.
    Maric, Selma
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Cárdenas, Marité
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Charaterising PC/cholesterol supported lipid bilayers and interactions with human HDL2017Ingår i: Acta Crystallographica Section A: Foundations and Advances, E-ISSN 2053-2733, Vol. 73, s. C105-C105Artikel i tidskrift (Övrigt vetenskapligt)
  • 42.
    Waldie, Sarah
    et al.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces. Institut Laue-Langevin, 71 Avenue des Martyrs, 38042 Grenoble, Cedex 9, France.
    Sebastiani, Federica
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Browning, Kathryn
    Department of Pharmacy, Copenhagen University, Universitetsparken 2, 2100 Copenhagen, Denmark.
    Maric, Selma
    MAX IV Laboratory, Fotongatan 2, 225 92 Lund, Sweden.
    Lind, Tania K
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Yepuri, Nageshwar
    National Deuteration Facility, Australian Nuclear Science and Technology Organisation, New Illawarra Road, Lucas Heights, NSW 2234, Australia.
    Darwish, Tamim A
    National Deuteration Facility, Australian Nuclear Science and Technology Organisation, New Illawarra Road, Lucas Heights, NSW 2234, Australia.
    Moulin, Martine
    Institut Laue-Langevin, 71 Avenue des Martyrs, 38042 Grenoble, Cedex 9, France.
    Strohmeier, Gernot
    Austrian Centre of Industrial Biotechnology, Petersgasse 14, 8010 Graz, Austria; Graz University of Technology, Institute of Organic Chemistry, NAWI Graz, Stremayrgasse 9, 8010 Graz, Austria.
    Pichler, Harald
    Austrian Centre of Industrial Biotechnology, Petersgasse 14, 8010 Graz, Austria; Graz University of Technology, Institute of Molecular Biotechnology, NAWI Graz, BioTechMed Graz, Petersgasse 14, 8010 Graz, Austria.
    Skoda, Maximilian W A
    STFC, Rutherford Appleton Laboratory, ISIS, Harwell, Didcot OX11 0QX, UK.
    Maestro, Armando
    Institut Laue-Langevin, 71 Avenue des Martyrs, 38042 Grenoble, Cedex 9, France.
    Haertlein, Michael
    Institut Laue-Langevin, 71 Avenue des Martyrs, 38042 Grenoble, Cedex 9, France.
    Forsyth, V Trevor
    Institut Laue-Langevin, 71 Avenue des Martyrs, 38042 Grenoble, Cedex 9, France; Faculty of Natural Sciences, Keele University, Staffordshire ST5 5BG, UK.
    Bengtsson, Eva
    Department of Clinical Sciences, Malmö, University of Lund, Clinical Research Center, Jan Waldenströms gata 35, 214 28 Malmö, Sweden.
    Malmsten, Martin
    Department of Pharmacy, Copenhagen University, Universitetsparken 2, 2100 Copenhagen, Denmark; Department of Physical Chemistry 1, University of Lund, SE-22100 Lund, Sweden.
    Cárdenas, Marité
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Lipoprotein ability to exchange and remove lipids from model membranes as a function of fatty acid saturation and presence of cholesterol.2020Ingår i: Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, ISSN 1388-1981, E-ISSN 1879-2618, Vol. 1865, nr 10, artikel-id 158769Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Lipoproteins play a central role in the development of atherosclerosis. High and low-density lipoproteins (HDL and LDL), known as 'good' and 'bad' cholesterol, respectively, remove and/or deposit lipids into the artery wall. Hence, insight into lipid exchange processes between lipoproteins and cell membranes is of particular importance in understanding the onset and development of cardiovascular disease. In order to elucidate the impact of phospholipid tail saturation and the presence of cholesterol in cell membranes on these processes, neutron reflection was employed in the present investigation to follow lipid exchange with both HDL and LDL against model membranes. Mirroring clinical risk factors for the development of atherosclerosis, lower exchange was observed in the presence of cholesterol, as well as for an unsaturated phospholipid, compared to faster exchange when using a fully saturated phospholipid. These results highlight the importance of membrane composition on the interaction with lipoproteins, chiefly the saturation level of the lipids and presence of cholesterol, and provide novel insight into factors of importance for build-up and reversibility of atherosclerotic plaque. In addition, the correlation between the results and well-established clinical risk factors suggests that the approach taken can be employed also for understanding a broader set of risk factors including, e.g., effects of triglycerides and oxidative stress, as well as local effects of drugs on atherosclerotic plaque formation.

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  • 43.
    Waldie, Sarah
    et al.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces. Institut Laue-Langevin, Grenoble, France; Partnership for Structural Biology (PSB), Grenoble, France.
    Sebastiani, Federica
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Moulin, Martine
    Institut Laue-Langevin, Grenoble, France; Partnership for Structural Biology (PSB), Grenoble, France.
    Del Giudice, Rita
    Malmö universitet, Biofilms Research Center for Biointerfaces. Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Paracini, Nicolò
    Malmö universitet, Biofilms Research Center for Biointerfaces. Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Roosen-Runge, Felix
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    Gerelli, Yuri
    Institut Laue-Langevin, Grenoble, France.
    Prevost, Sylvain
    Institut Laue-Langevin, Grenoble, France; Department of Life and Environmental Sciences, Marche Polytechnic University, Ancona, Italy.
    Voss, John C.
    Department of Biochemistry and Molecular Medicine, University of California, Davis, Davis, CA, United States.
    Darwish, Tamim A.
    National Deuteration Facility, Australian Nuclear Science and Technology Organisation, Lucas Heights, NSW, Australia.
    Yepuri, Nageshwar
    National Deuteration Facility, Australian Nuclear Science and Technology Organisation, Lucas Heights, NSW, Australia.
    Pichler, Harald
    Austrian Centre of Industrial Biotechnology, Graz, Austria; Graz University of Technology, Institute of Molecular Biotechnology, NAWI Graz, BioTechMed Graz, Graz, Austria.
    Maric, Selma
    MAX IV Laboratory, Lund, Sweden.
    Forsyth, V. Trevor
    Institut Laue-Langevin, Grenoble, France; Partnership for Structural Biology (PSB), Grenoble, France; Faculty of Natural Sciences, Keele University, Staffordshire, United Kingdom.
    Haertlein, Michael
    Institut Laue-Langevin, Grenoble, France; Partnership for Structural Biology (PSB), Grenoble, France.
    Cárdenas, Marité
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV). Malmö universitet, Biofilms Research Center for Biointerfaces.
    ApoE and ApoE Nascent-Like HDL Particles at Model Cellular Membranes: Effect of Protein Isoform and Membrane Composition2021Ingår i: Frontiers in Chemistry, E-ISSN 2296-2646, Vol. 9, artikel-id 630152Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Apolipoprotein E (ApoE), an important mediator of lipid transportation in plasma and the nervous system, plays a large role in diseases such as atherosclerosis and Alzheimer's. The major allele variants ApoE3 and ApoE4 differ only by one amino acid. However, this difference has major consequences for the physiological behaviour of each variant. In this paper, we follow (i) the initial interaction of lipid-free ApoE variants with model membranes as a function of lipid saturation, (ii) the formation of reconstituted High-Density Lipoprotein-like particles (rHDL) and their structural characterisation, and (iii) the rHDL ability to exchange lipids with model membranes made of saturated lipids in the presence and absence of cholesterol [1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) or 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine (POPC) with and without 20 mol% cholesterol]. Our neutron reflection results demonstrate that the protein variants interact differently with the model membranes, adopting different protein conformations. Moreover, the ApoE3 structure at the model membrane is sensitive to the level of lipid unsaturation. Small-angle neutron scattering shows that the ApoE containing lipid particles form elliptical disc-like structures, similar in shape but larger than nascent or discoidal HDL based on Apolipoprotein A1 (ApoA1). Neutron reflection shows that ApoE-rHDL do not remove cholesterol but rather exchange saturated lipids, as occurs in the brain. In contrast, ApoA1-containing particles remove and exchange lipids to a greater extent as occurs elsewhere in the body.

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  • 44.
    Wared, Mary
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Validering av vankomycin-resistenta enterokocker: Diagnostik på panther fusion open access instrument2022Självständigt arbete på grundnivå (kandidatexamen), 10 poäng / 15 hpStudentuppsats (Examensarbete)
    Abstract [sv]

    Panther Fusion® system är ett fullständigt automatiserat in vitro diagnostiksystem som har högt flöde av prov-till-resultat och tillåter utförandet av in vitro diagnostiska tester genom användning av realtids Polymerase Chain Reaction (realtids-PCR). Syftet med detta projekt är att validera om det finns möjlighet att använda ett kit från Amplidiag på Panther fusion open access för att diagnostisera vankomycin resistenta enterokocker (VRE) samt att utvärdera analys direkt på E-swab prover istället för anrikningsbuljong. Det är viktigt att kunna detektera vanA-och vanB-generna i prover för att VRE hyser dessa gener. Sensitivitet och effektivitet av Panther fusion open access undersöktes genom att analysera proverna parallellt med Bio-Rad CFX384/96-PCR som är rutinmetoden för VRE-diagnostik på Klinisk mikrobiologi i Lund. Specificitet av en tidigare publicerad PCR-mix (PCR-mix) som kan detektera vanA och vanB i prover jämfördes med Amplidiag assay mix 2 som används i rutinmetoden. För att kunna utvärdera skillnaden av specificiteten och känsligheten mellan E-swab och anrikningsbuljong utfördes analysen på både E-swab och anrikningsbulong med både Panther fusion open access och Bio-Rad CFX384/96-PCR. MgCl2- koncentration optimerades till 3,0 mM. Sensitivitet och effektivitet av Panther fusion open access var högre med PCR-mix än Amplidiag assay mix 2 och uppvisade optimalt linjäritet. Specificitetstest av PCR-mixen visade att den bara kunde detektera vanA och vanB. Resultaten av spikade VRE-negativa patientprover (E-swab) visade sig vara orimliga då flera av proverna och kontrollerna gav resultat för båda generna. För att ersätta VRE-diagnostik på Bio-Rad CFX384/96 med Panther fusion open access behöver ytterligare experiment genomföras direkt på E-swab och vankomycine variabla enterokocker (VVE)-prover på Panther fusion open access.

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