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Photo Lynn Kamerlin

Lynn Kamerlin

Professor

Photo Lynn Kamerlin

Amyloid-β Peptide Interactions with Amphiphilic Surfactants : Electrostatic and Hydrophobic Effects

Author

  • Nicklas Österlund
  • Yashraj S Kulkarni
  • Agata D Misiaszek
  • Cecilia Wallin
  • Dennis M Krüger
  • Qinghua Liao
  • Farshid Mashayekhy Rad
  • Jüri Jarvet
  • Birgit Strodel
  • Sebastian K T S Wärmländer
  • Leopold L Ilag
  • Shina C L Kamerlin
  • Astrid Gräslund
Show all

Summary, in English

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.

Publishing year

2018-07-18

Language

English

Pages

1680-1692

Publication/Series

ACS Chemical Neuroscience

Volume

9

Issue

7

Document type

Journal article

Publisher

The American Chemical Society (ACS)

Keywords

  • Amyloid beta-Peptides/chemistry
  • Animals
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Micelles
  • Molecular Dynamics Simulation
  • Protein Aggregation, Pathological/drug therapy
  • Protein Structure, Secondary
  • Static Electricity
  • Surface-Active Agents/chemistry

Status

Published

ISBN/ISSN/Other

  • ISSN: 1948-7193