TY  - JOUR
AU  - Dogan, Susanne
AU  - Paulus, Michael
AU  - Forov, Yury
AU  - Weis, Christopher
AU  - Kampmann, Matthias
AU  - Cewe, Christopher
AU  - Kiesel, Irena
AU  - Degen, Patrick
AU  - Salmen, Paul
AU  - Rehage, Heinz
AU  - Tolan, Metin
TI  - Human Apolipoprotein A1 at Solid/Liquid and Liquid/Gas Interfaces
JO  - The journal of physical chemistry  / B
VL  - 122
IS  - 14
SN  - 1089-5647
CY  - Washington, DC
PB  - ACS
M1  - PUBDB-2019-00209
SP  - 3953 - 3960
PY  - 2018
N1  - © American Chemical Society; Post referee fulltext in progress 2; Embargo 12 months from publication
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:29488751
UR  - <Go to ISI:>//WOS:000430641900026
DO  - DOI:10.1021/acs.jpcb.7b12481
UR  - https://bib-pubdb1.desy.de/record/418122
ER  -