%0 Journal Article
%A Österlund, Nicklas
%A Kulkarni, Yashraj S.
%A Misiaszek, Agata D.
%A Wallin, Cecilia
%A Krüger, Dennis M.
%A Liao, Qinghua
%A Mashayekhy Rad, Farshid
%A Jarvet, Jüri
%A Strodel, Birgit
%A Wärmländer, Sebastian K. T. S.
%A Ilag, Leopold L.
%A Kamerlin, Shina C. L.
%A Gräslund, Astrid
%T Amyloid-β Peptide Interactions with Amphiphilic Surfactants: Electrostatic and Hydrophobic Effects
%J ACS chemical neuroscience
%V 9
%N 7
%@ 1948-7193
%C Washington, DC
%I ACS Publ.
%M FZJ-2018-07744
%P 1680 - 1692
%D 2018
%X The amphiphilic nature of the amyloid-β (Aβ) peptide associated with Alzheimer's disease facilitates various interactions with biomolecules such as lipids and proteins, with effects on both structure and toxicity of the peptide. Here, we investigate these peptide-amphiphile interactions by experimental and computational studies of Aβ(1-40) in the presence of surfactants with varying physicochemical properties. Our findings indicate that electrostatic peptide-surfactant interactions are required for coclustering and structure induction in the peptide and that the strength of the interaction depends on the surfactant net charge. Both aggregation-prone peptide-rich coclusters and stable surfactant-rich coclusters can form. Only Aβ(1-40) monomers, but not oligomers, are inserted into surfactant micelles in this surfactant-rich state. Surfactant headgroup charge is suggested to be important as electrostatic peptide-surfactant interactions on the micellar surface seems to be an initiating step toward insertion. Thus, no peptide insertion or change in peptide secondary structure is observed using a nonionic surfactant. The hydrophobic peptide-surfactant interactions instead stabilize the Aβ monomer, possibly by preventing self-interaction between the peptide core and C-terminus, thereby effectively inhibiting the peptide aggregation process. These findings give increased understanding regarding the molecular driving forces for Aβ aggregation and the peptide interaction with amphiphilic biomolecules.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:29683649
%U <Go to ISI:>//WOS:000439531400017
%R 10.1021/acschemneuro.8b00065
%U https://juser.fz-juelich.de/record/858908