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  • 1. Browning, Kathryn
    et al.
    Lind, Tania
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Maric, Selma
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Malekkhaiat-Haffner, Sara
    Fredrikson, Gunilla
    Bengtsson, Eva
    Malmsten, Martin
    Cárdenas, Marité
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Human lipoproteins at model cell membranes: Role of the lipoprotein class on lipid dynamics2017In: Abstracts of Papers of the American Chemical Society, ISSN 0065-7727, Vol. 253Article in journal (Other academic)
  • 2. Browning, Kathryn Louise
    et al.
    Lind, Tania Kjellerup
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Maric, Selma
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Barker, Robert David
    Cárdenas, Marité
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Malmsten, Martin
    Effect of bilayer charge on lipoprotein lipid exchange2018In: Colloids and Surfaces B: Biointerfaces, ISSN 0927-7765, E-ISSN 1873-4367, Vol. 168, p. 117-125Article in journal (Refereed)
    Abstract [en]

    Lipoproteins play a key role in the onset and development of atherosclerosis, the formation of lipid plaques at blood vessel walls. The plaque formation, as well as subsequent calcification, involves not only endothelial cells but also connective tissue, and is closely related to a wide range of cardiovascular syndromes, that together constitute the number one cause of death in the Western World. High (HDL) and low (LDL) density lipoproteins are of particular interest in relation to atherosclerosis, due to their protective and harmful effects, respectively. In an effort to elucidate the molecular mechanisms underlying this, and to identify factors determining lipid deposition and exchange at lipid membranes, we here employ neutron reflection (NR) and quartz crystal microbalance with dissipation (QCM-D) to study the effect of membrane charge on lipoprotein deposition and lipid exchange. Dimyristoylphosphatidylcholine (DMPC) bilayers containing varying amounts of negatively charged dimyristoylphosphatidylserine (DMPS) were used to vary membrane charge. It was found that the amount of hydrogenous material deposited from either HDL or LDL to the bilayer depends only weakly on membrane charge density. In contrast, increasing membrane charge resulted in an increase in the amount of lipids removed from the supported lipid bilayer, an effect particularly pronounced for LDL. The latter effects are in line with previously reported observations on atherosclerotic plaque prone regions of long-term hyperlipidaemia and type 2 diabetic patients, and may also provide some molecular clues into the relation between oxidative stress and atherosclerosis. (C) 2018 Elsevier B.V. All rights reserved.

  • 3.
    Browning, T. K.
    et al.
    Department of Pharmacy, Uppsala University, Uppsala, Sweden.
    Lind, Tania Kjellerup
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Maric, Selma
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Malekkhaiat-Häffner, S.
    Department of Pharmacy, Uppsala University, Uppsala, Sweden.
    Fredrikson, G. N.
    Department of Clinical Sciences, Malmö, Lund University, Malmö, Sweden.
    Bengtsson, E.
    Department of Clinical Sciences, Malmö, Lund University, Malmö, Sweden.
    Malmsten, M.
    Department of Pharmacy, Uppsala University, Uppsala, Sweden; Department of Pharmacy, University of Copenhagen, Copenhagen, Denmark.
    Cárdenas, Marité
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Human lipoproteins at model cell membranes: Role of the lipoprotein class on lipid dynamics2017In: Scientific Reports, E-ISSN 2045-2322, Vol. 7, article id 7478Article in journal (Refereed)
    Abstract [en]

    High and low density lipoproteins (HDL and LDL) are thought to play vital roles in the onset and development of atherosclerosis; the biggest killer in the western world. Key issues of initial lipoprotein (LP) interactions at cellular membranes need to be addressed including LP deposition and lipid exchange. Here we present a protocol for monitoring the in situ kinetics of lipoprotein deposition and lipid exchange/removal at model cellular membranes using the non-invasive, surface sensitive methods of neutron reflection and quartz crystal microbalance with dissipation. For neutron reflection, lipid exchange and lipid removal can be distinguished thanks to the combined use of hydrogenated and tail-deuterated lipids. Both HDL and LDL remove lipids from the bilayer and deposit hydrogenated material into the lipid bilayer, however, the extent of removal and exchange depends on LP type. These results support the notion of HDL acting as the ‘good’ cholesterol, removing lipid material from lipid-loaded cells, whereas LDL acts as the ‘bad’ cholesterol, depositing lipid material into the vascular wall.

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  • 4. Jagalski, Vivien
    et al.
    Barker, Robert
    Thygesen, Mikkel B.
    Gotfryd, Kamil
    Krüger, Mie B.
    Shi, Lei
    Bovet, Nicolas
    Moulin, Martine
    Haertlein, Michael
    Günther Pomorski, Thomas
    Loland, Claus J
    Maric, Selma
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Grafted Biomembranes Containing Membrane Proteins: The Case for the Leucine Transporter2015In: Soft Matter, ISSN 1744-683X, E-ISSN 1744-6848, Vol. 11, no 39, p. 7707-7711Article in journal (Refereed)
    Abstract [en]

    Here, we bind the sodium dependent amino acid transporter on nitrilotriacetic acid/polyethylene glycol functionalized gold sensors in detergents and perform a detergent–lipid exchange with phosphatidylcholine. We characterize the LeuT structure in the adsorbed film by magnetic contrast neutron reflection using the predicted model from molecular dynamic simulations.

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  • 5. Josts, Inokentijs
    et al.
    Nitsche, Julius
    Maric, Selma
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Mertens, Haydyn D.
    Moulin, Martine
    Haertlein, Michael
    Prevost, Sylvain
    Svergun, Dmitri I.
    Busch, Sebastian
    Forsyth, V. Trevor
    Tidow, Henning
    Conformational States of ABC Transporter MsbA in a Lipid Environment Investigated by Small-Angle Scattering Using Stealth Carrier Nanodiscs2018In: Structure, ISSN 0969-2126, E-ISSN 1878-4186, Vol. 26, no 8, p. 1072-1079.e4Article in journal (Refereed)
    Abstract [en]

    Structural studies of integral membrane proteins (IMPs) are challenging, as many of them are inactive or insoluble in the absence of a lipid environment. Here, we describe an approach making use of fractionally deuterium labeled "stealth carrier'' nanodiscs that are effectively invisible to low-resolution neutron diffraction and enable structural studies of IMPs in a lipidic native-like solution environment. We illustrate the potential of the method in a joint small-angle neutron scattering (SANS) and X-ray scattering (SAXS) study of the ATP-binding cassette (ABC) transporter protein MsbA solubilized in the stealth nanodiscs. The data allow for a direct observation of the signal from the solubilized protein without contribution from the surrounding lipid nanodisc. Not only the overall shape but also differences between conformational states of MsbA can be reliably detected from the scattering data, demonstrating the sensitivity of the approach and its general applicability to structural studies of IMPs.

  • 6.
    Maric, Selma
    et al.
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Lind, Tania
    Cárdenas, Marité
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Lipoprotein structure dependency on its lipid cargo and exchange dynamics: Implications for atherosclerosis development2016In: Abstracts of Papers of the American Chemical Society, ISSN 0065-7727, Vol. 251Article in journal (Other academic)
  • 7.
    Maric, Selma
    et al.
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Lind, Tania Kjellerup
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Lyngso, Jeppe
    Bengtsson, Eva
    Fredrikson, Gunilla
    Moulin, Martine
    Haertlein, Michael
    Forsyth, Trevor
    Pedersen, Jan Skov
    Cárdenas, Marité
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Lipoprotein structure dependency on lipid cargo and exchange dynamics: Implications for atherosclerosis development2017In: Abstracts of Papers of the American Chemical Society, ISSN 0065-7727, Vol. 253Article in journal (Other academic)
  • 8.
    Maric, Selma
    et al.
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Lind, Tania Kjellerup
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Lyngsø, Jeppe
    Cárdenas, Marité
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Skov Pedersen, Jan
    Modeling Small-Angle X-Ray Scattering Data for Low Density Lipoproteins: Insights Into The Fatty Core Phase Packing And Transition2017In: ACS Nano, ISSN 1936-0851, E-ISSN 1936-086X, Vol. 11, no 1, p. 1080-1090Article in journal (Refereed)
    Abstract [en]

    Atherosclerosis and its clinical consequences are the leading cause of death in the western hemisphere. While many studies throughout the last decades have aimed at understanding the disease, the clinical markers in use today still fail to accurately predict the risks. The role of the current main clinical indicator, low density lipoprotein (LDL), in depositing fat to the vessel wall is believed to be the onset of the process. However, many subfractions of the LDL, which differ both in structure and composition, are present in the blood and among different individuals. Understanding the relationship between LDL structure and composition is key to unravel the specific role of various LDL components in the development and/or prevention of atherosclerosis. Here, we describe a model for analyzing small-angle X-ray scattering data for rapid and robust structure determination for the LDL. The model not only gives the overall structure but also the particular internal layering of the fats inside the LDL core. Thus, the melting of the LDL can be followed in situ as a function of temperature for samples extracted from healthy human patients and purified using a double protocol based on ultracentrifugation and size-exclusion chromatography. The model provides information on: (i) the particle-specific melting temperature of the core lipids, (ii) the structural organization of the core fats inside the LDL, (iii) the overall shape of the particle, and (iv) the flexibility and overall conformation of the outer protein/hydrophilic layer at a given temperature as governed by the organization of the core. The advantage of this method over other techniques such as cryo-TEM is the possibility of in situ experiments under near-physiological conditions which can be performed relatively fast (minutes at home source, seconds at synchrotron). This approach now allows the monitoring of structural changes in the LDL upon different stresses from the environment, such as changes in temperature, oxidation, or external agents used or currently in development against atherosclerotic plaque build-up and which are targeting the LDL.

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  • 9.
    Maric, Selma
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Lind, Tania Kjellerup
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Raida, Manfred Roman
    Singapore Lipidomics Incubator (SLING), Life Sciences Institute, National University of Singapore, Singapore, Singapore.
    Bengtsson, Eva
    Dept. of Clinical Sciences, Lund University, Jan Waldenströms gata 35, CRC, Box 50332, 212 13, Malmö, Sweden.
    Fredrikson, Gunilla Nordin
    Dept. of Clinical Sciences, Lund University, Jan Waldenströms gata 35, CRC, Box 50332, 212 13, Malmö, Sweden.
    Rogers, Sarah
    ISIS Science and Technology Facilities Council, Harwell Science and Innovation Campus, Chilton, Didcot, Oxfordshire, OX11 0QX, United Kingdom.
    Moulin, Martine
    Life Science Group, Institut Laue Langevin, 6, rue Jules Horowitz, BP 156, F-38042, Grenoble, Cedex 9, France.
    Haertlein, Michael
    Life Science Group, Institut Laue Langevin, 6, rue Jules Horowitz, BP 156, F-38042, Grenoble, Cedex 9, France.
    Forsyth, V. Trevor
    Life Science Group, Institut Laue Langevin, 6, rue Jules Horowitz, BP 156, F-38042, Grenoble, Cedex 9, France; Faculty of Natural Science and Institute for Science and Technology in Medicine, Keele University, Staffordshire, ST5 5BG, United Kingdom.
    Wenk, Markus R.
    Singapore Lipidomics Incubator (SLING), Life Sciences Institute, National University of Singapore, Singapore, Singapore.
    Pomorski, Thomas Guenther
    Dept. of Plant and Environmental Sciences, University of Copenhagen, Thorvaldsensvej 40, 1871, Frederiksberg C, Denmark; Dept. of Molecular Biochemistry, Ruhr University Bochum, Faculty of Chemistry and Biochemistry, 44780, Bochum, Germany.
    Arnebrant, Thomas
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Lund, Reidar
    Dept. of Chemistry, University of Oslo, Blindern, 0315, Oslo, Norway.
    Cárdenas, Marité
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Time-resolved small-angle neutron scattering as a probe for the dynamics of lipid exchange between human lipoproteins and naturally derived membranes2019In: Scientific Reports, E-ISSN 2045-2322, Vol. 9, no 1, article id 7591Article in journal (Refereed)
    Abstract [en]

    Atherosclerosis is the main killer in the western world. Today's clinical markers include the total level of cholesterol and high-/low-density lipoproteins, which often fails to accurately predict the disease. The relationship between the lipid exchange capacity and lipoprotein structure should explain the extent by which they release or accept lipid cargo and should relate to the risk for developing atherosclerosis. Here, small-angle neutron scattering and tailored deuteration have been used to follow the molecular lipid exchange between human lipoprotein particles and cellular membrane mimics made of natural, "neutron invisible" phosphatidylcholines. We show that lipid exchange occurs via two different processes that include lipid transfer via collision and upon direct particle tethering to the membrane, and that high-density lipoprotein excels at exchanging the human-like unsaturated phosphatidylcholine. By mapping the specific lipid content and level of glycation/oxidation, the mode of action of specific lipoproteins can now be deciphered. This information can prove important for the development of improved diagnostic tools and in the treatment of atherosclerosis.

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  • 10. Moulin, Martine
    et al.
    Strohmeier, Gernot A.
    Hirz, Melanie
    Thompson, Katherine C.
    Rennie, Adrian R.
    Campbell, Richard A.
    Pichler, Harald
    Maric, Selma
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Forsyth, V. Trevor
    Haertlein, Michael
    Perdeuteration of cholesterol for neutron scattering applications using recombinant Pichia pastoris2018In: Chemistry and Physics of Lipids, ISSN 0009-3084, E-ISSN 1873-2941, Vol. 212, p. 80-87Article in journal (Refereed)
    Abstract [en]

    Deuteration of biomolecules has a major impact on both quality and scope of neutron scattering experiments. Cholesterol is a major component of mammalian cells, where it plays a critical role in membrane permeability, rigidity and dynamics, and contributes to specific membrane structures such as lipid rafts. Cholesterol is the main cargo in low and high-density lipoprotein complexes (i.e. LDL, HDL) and is directly implicated in several pathogenic conditions such as coronary artery disease which leads to 17 million deaths annually. Neutron scattering studies on membranes or lipid-protein complexes exploiting contrast variation have been limited by the lack of availability of fully deuterated biomolecules and especially perdeuterated cholesterol. The availability of perdeuterated cholesterol provides a unique way of probing the structural and dynamical properties of the lipoprotein complexes that underly many of these disease conditions. Here we describe a procedure for in vivo production of perdeuterated recombinant cholesterol in lipid-engineered Pichia pastoris using flask and fed batch fermenter cultures in deuterated minimal medium. Perdeuteration of the purified cholesterol was verified by mass spectrometry and its use in a neutron scattering study was demonstrated by neutron reflectometry measurements using the FIGARO instrument at the ILL.

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  • 11. Nitsche, Julius
    et al.
    Josts, Inokentijs
    Heidemann, Johannes
    Mertens, Haydyn D
    Maric, Selma
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Moulin, Martine
    Haertlein, Michael
    Busch, Sebastian
    Forsyth, V Trevor
    Svergun, Dmitri I
    Uetrecht, Charlotte
    Tidow, Henning
    Structural basis for activation of plasma-membrane Ca(2+)-ATPase by calmodulin.2018In: Communications Biology, E-ISSN 2399-3642, Vol. 1, article id 206Article in journal (Refereed)
    Abstract [en]

    Plasma-membrane Ca(2+)-ATPases expel Ca(2+) from the cytoplasm and are key regulators of Ca(2+) homeostasis in eukaryotes. They are autoinhibited under low Ca(2+) concentrations. Calmodulin (CaM)-binding to a unique regulatory domain releases the autoinhibition and activates the pump. However, the structural basis for this activation, including the overall structure of this calcium pump and its complex with calmodulin, is unknown. We previously determined the high-resolution structure of calmodulin in complex with the regulatory domain of the plasma-membrane Ca(2+)-ATPase ACA8 and revealed a bimodular mechanism of calcium control in eukaryotes. Here we show that activation of ACA8 by CaM involves large conformational changes. Combining advanced modeling of neutron scattering data acquired from stealth nanodiscs and native mass spectrometry with detailed dissection of binding constants, we present a structural model for the full-length ACA8 Ca(2+) pump in its calmodulin-activated state illustrating a displacement of the regulatory domain from the core enzyme.

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  • 12.
    Waldie, Sarah Hannah Anne
    et al.
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Browning, Kathryn
    Moulin, Martine
    Haertlein, Michael
    Forsyth, Trevor
    Maric, Selma
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Cárdenas, Marité
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Charaterising PC/cholesterol supported lipid bilayers and interactions with human HDL2017In: Acta Crystallographica Section A: Foundations and Advances, E-ISSN 2053-2733, Vol. 73, p. C105-C105Article in journal (Other academic)
  • 13.
    Waldie, Sarah
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Lind, Tania K
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Browning, Kathrin
    Moulin, Martine
    Haertlein, Michael
    Forsyth, Trevor
    Luchini, Alessandra
    Strohmeier, Gernot A
    Harald, Pichler
    Maric, Selma
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Cárdenas, Marité
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Localization of Cholesterol within Supported Lipid Bilayers Made of a Natural Extract of Tailor-Deuterated Phosphatidylcholine2018In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 34, no 1, p. 472-479Article in journal (Refereed)
    Abstract [en]

    Cholesterol is an essential component of mammalian membranes and is known to induce a series of physicochemical changes in the lipid bilayer. Such changes include the formation of liquid-ordered phases with an increased thickness and a configurational order as compared to liquid-disordered phases. For saturated lipid membranes, cholesterol molecules localize close to the lipid head group-tail interface. However, the presence of polyunsaturated lipids was recently shown to promote relocation of cholesterol toward the inner interface between the two bilayer leaflets. Here, neutron reflection is used to study the location of cholesterol (both non-deuterated and per-deuterated versions are used) within supported lipid bilayers composed of a natural mixture of phosphatidylcholine (PC). The lipids were produced in a genetically modified strain of Escherichia coli and grown under specific deuterated conditions to give an overall neutron scattering length density (which depends on the level of deuteration) of the lipids matching that of D2O. The combination of solvent contrast variation method with specific deuteration shows that cholesterol is located closer to the lipid head group-tail interface in this natural PC extract rather than in the center of the core of the bilayer as seen for very thin or polyunsaturated membranes.

  • 14.
    Waldie, Sarah
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Moulin, Martine
    Porcar, Lionel
    Pichler, Harald
    Strohmeier, Gernot A
    Skoda, Maximilian
    Forsyth, V Trevor
    Haertlein, Michael
    Maric, Selma
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Cárdenas, Marité
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    The Production of Matchout-Deuterated Cholesterol and the Study of Bilayer-Cholesterol Interactions2019In: Scientific Reports, E-ISSN 2045-2322, Vol. 9, no 1, article id 5118Article in journal (Refereed)
    Abstract [en]

    The deuteration of biomolecules provides advanced opportunities for neutron scattering studies. For low resolution studies using techniques such as small-angle neutron scattering and neutron reflection, the level of deuteration of a sample can be varied to match the scattering length density of a specific DO/HO solvent mixture. This can be of major value in structural studies where specific regions of a complex system can be highlighted, and others rendered invisible. This is especially useful in analyses of the structure and dynamics of membrane components. In mammalian membranes, the presence of cholesterol is crucial in modulating the properties of lipids and in their interaction with proteins. Here, a protocol is described for the production of partially deuterated cholesterol which has a neutron scattering length density that matches that of 100% DO solvent (hereby named matchout cholesterol). The level of deuteration was determined by mass spectrometry and nuclear magnetic resonance. The cholesterol match-point was verified experimentally using small angle neutron scattering. The matchout cholesterol was used to investigate the incorporation of cholesterol in various phosphatidylcholine supported lipid bilayers by neutron reflectometry. The study included both saturated and unsaturated lipids, as well as lipids with varying chain lengths. It was found that cholesterol is distributed asymmetrically within the bilayer, positioned closer to the headgroups of the lipids than to the middle of the tail core, regardless of the phosphatidylcholine species.

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  • 15.
    Waldie, Sarah
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Sebastiani, Federica
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Browning, Kathryn
    Maric, Selma
    Lind, Tania K
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Yepuri, Nageshwar
    Darwish, Tamim A
    Moulin, Martine
    Strohmeier, Gernot
    Pichler, Harald
    Skoda, Maximilian W A
    Maestro, Armando
    Haertlein, Michael
    Forsyth, V Trevor
    Bengtsson, Eva
    Malmsten, Martin
    Cárdenas, Marité
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, 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.2020In: Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, ISSN 1388-1981, E-ISSN 1879-2618, Vol. 1865, no 10, article id 158769Article in journal (Refereed)
    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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