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Amyloid-beta Peptide Interactions with Amphiphilic Surfactants: Electrostatic and Hydrophobic Effects
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Faculty of Science, Department of Environmental Science and Analytical Chemistry.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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Number of Authors: 132018 (English)In: ACS Chemical Neuroscience, ISSN 1948-7193, E-ISSN 1948-7193, Vol. 9, no 7, p. 1680-1692Article in journal (Refereed) Published
Abstract [en]

The amphiphilic nature of the amyloid-beta (A beta) 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 A beta(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 A beta(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 A beta 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 A beta aggregation and the peptide interaction with amphiphilic biomolecules.

Place, publisher, year, edition, pages
2018. Vol. 9, no 7, p. 1680-1692
Keywords [en]
Alzheimer's disease, A beta aggregation, surfactant interactions, optical and NMR spectroscopy, mass spectrometry, molecular dynamics simulations
National Category
Neurosciences Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-159131DOI: 10.1021/acschemneuro.8b00065ISI: 000439531400017PubMedID: 29683649OAI: oai:DiVA.org:su-159131DiVA, id: diva2:1243213
Available from: 2018-08-30 Created: 2018-08-30 Last updated: 2020-03-05Bibliographically approved

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Österlund, NicklasWallin, CeciliaMashayekhy Rad, FarshidJarvet, JüriStrodel, BirgitWärmländer, Sebastian K. T. S.Ilag, Leopold L.Gräslund, Astrid
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Department of Biochemistry and BiophysicsDepartment of Environmental Science and Analytical Chemistry
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