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    Human Apolipoprotein Al at Solid/Liquid and Liquid/Gas Interfaces

    Year: 2018

    Journal: J. Phys. Chem. B, Volume 122, APR 12, page 3953–3960

    Authors: Dogan, Susanne; Paulus, Michael; Forov, Yury; Weis, Christopher; Kampmann, Matthias; Cewe, Christopher; Kiesel, Irena; Degen, Patrick; Salmen, Paul; Rehage, Heinz; Tolan, Metin

    Organizations: NMI3-II Grant [283883]; DFG [FOR1979]; Cluster of Excellence RESOLV [EXC 1069]

    An X-ray reflectivity study on the adsorption behavior of human apolipoprotein Al (apoAl) 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 apoAl to include lipids, resulting in a depletion of the lipids from the interface.
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