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000418122 0247_ $$2doi$$a10.1021/acs.jpcb.7b12481
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000418122 0247_ $$2ISSN$$a1541-5740
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000418122 1001_ $$0P:(DE-H253)PIP1030185$$aDogan, Susanne$$b0$$eCorresponding author
000418122 245__ $$aHuman Apolipoprotein A1 at Solid/Liquid and Liquid/Gas Interfaces
000418122 260__ $$aWashington, DC$$bACS$$c2018
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000418122 520__ $$aAn X-ray reflectivity study on the adsorption behavior of human apolipoprotein A1 (apoA1) at hydrophilic and hydrophobic interfaces is presented. It is shown that the protein interacts via electrostatic and hydrophobic interactions with the interfaces, resulting in the absorption of the protein. pH dependent measurements at the solid/liquid interface between silicon dioxide and aqueous protein solution show that in a small pH range between pH 4 and 6, adsorption is increased due to electrostatic attraction. Here, the native shape of the protein seems to be conserved. In contrast, the adsorption at the liquid/gas interface is mainly driven by hydrophobic effects, presumably by extending the hydrophobic regions of the amphipathic helices, and results in a conformational change of the protein during adsorption. However, the addition of differently charged membrane-forming lipids at the liquid/gas interface illustrates the ability of apoA1 to include lipids, resulting in a depletion of the lipids from the interface.
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000418122 7001_ $$0P:(DE-H253)PIP1007931$$aPaulus, Michael$$b1$$eCorresponding author
000418122 7001_ $$aForov, Yury$$b2
000418122 7001_ $$aWeis, Christopher$$b3
000418122 7001_ $$aKampmann, Matthias$$b4
000418122 7001_ $$aCewe, Christopher$$b5
000418122 7001_ $$aKiesel, Irena$$b6
000418122 7001_ $$aDegen, Patrick$$b7
000418122 7001_ $$aSalmen, Paul$$b8
000418122 7001_ $$aRehage, Heinz$$b9
000418122 7001_ $$0P:(DE-H253)PIP1007936$$aTolan, Metin$$b10
000418122 773__ $$0PERI:(DE-600)2006039-7$$a10.1021/acs.jpcb.7b12481$$gVol. 122, no. 14, p. 3953 - 3960$$n14$$p3953 - 3960$$tThe journal of physical chemistry <Washington, DC> / B$$v122$$x1089-5647$$y2018
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