Journal Article PUBDB-2019-00209

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Human Apolipoprotein A1 at Solid/Liquid and Liquid/Gas Interfaces

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2018
ACS Washington, DC

The journal of physical chemistry <Washington, DC> / B 122(14), 3953 - 3960 () [10.1021/acs.jpcb.7b12481]
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Abstract: An 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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Note: © American Chemical Society; Post referee fulltext in progress 2; Embargo 12 months from publication

Contributing Institute(s):
  1. DOOR-User (DOOR)
Research Program(s):
  1. 899 - ohne Topic (POF3-899) (POF3-899)
Experiment(s):
  1. DORIS Beamline BW1 (DORIS III)

Appears in the scientific report 2018
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 Record created 2019-01-09, last modified 2025-07-29


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