uu.seUppsala University Publications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Amyloid-beta Peptide Interactions with Amphiphilic Surfactants: Electrostatic and Hydrophobic Effects
Stockholm Univ, Dept Biochem & Biophys, Arrhenius Labs, S-10691 Stockholm, Sweden;Stockholm Univ, Dept Environm Sci & Analyt Chem, Arrhenius Labs, S-10691 Stockholm, Sweden.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
Stockholm Univ, Dept Biochem & Biophys, Arrhenius Labs, S-10691 Stockholm, Sweden.ORCID iD: 0000-0003-4464-1769
Show others and affiliations
2018 (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
AMER CHEMICAL SOC , 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
Identifiers
URN: urn:nbn:se:uu:diva-386225DOI: 10.1021/acschemneuro.8b00065ISI: 000439531400017PubMedID: 29683649OAI: oai:DiVA.org:uu-386225DiVA, id: diva2:1327238
Funder
Swedish Research CouncilAvailable from: 2019-06-19 Created: 2019-06-19 Last updated: 2019-06-19Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textPubMed

Authority records BETA

Kulkarni, Yashraj S.Liao, QinghuaKamerlin, Shina C. L.

Search in DiVA

By author/editor
Kulkarni, Yashraj S.Wallin, CeciliaLiao, QinghuaStrodel, BirgitKamerlin, Shina C. L.
By organisation
Structural BiologyDepartment of Cell and Molecular Biology
In the same journal
ACS Chemical Neuroscience
Neurosciences

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 46 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf