Peptide-surfactant interactions: Consequences for the amyloid-beta structure

• Type: Article in International Scientific Journal
• Date: 2012

Authors

Sandra Rocha (Author) FEUP; Joana A. Loureiro (Author) FEUP; Gerald Brezesinski (Author) Other; Maria do Carmo Pereira (Author) FEUP

Journal

Title: Biochemical and Biophysical Research Communications

Vol. 420 No. 1

Pages: 136-140

ISSN: 0006-291X

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 18 Citations

Scopus - 19 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

CORDIS: Health sciences ; Technological sciences

Associated Projects

Referência: PTDC/QUI-BIQ/102827/2008 - Concepção de péptidos fluorados para inibição da agregação do péptido beta-amilóide e avaliação da sua actividade biológica

Other information

Authenticus ID: P-002-BYW

DOI: 10.1016/j.bbrc.2012.02.129

Abstract (EN): The conformation of amyloid-beta peptide (A beta) determines if toxic aggregates are formed. The peptide structure by its turn depends on the environment and molecule-molecule interactions. We characterized the secondary structure of A beta-(1-40) in surfactant solutions and interacting with monolayers. The peptide adopts beta-sheet structure in solutions of ionic surfactants at sub-micelle concentrations and alpha-helix in the presence of ionic micelles. Uncharged micelles induce beta-sheets. A beta-(1-40) alters the critical micelle concentration value of the non-ionic surfactant, underlining hydrophobic interactions. At ionic monolayers the peptide forms beta-sheets when its concentration at the surface is high enough. These results suggest that only electrostatic interactions of charged micelles that surround completely the peptide are able to induce non-aggregated a-helix structure.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 5