Please use this identifier to cite or link to this item: https://hdl.handle.net/10216/104617
Author(s): Sandra Rocha
Joana A. Loureiro
Gerald Brezesinski
Maria do Carmo Pereira
Title: Peptide-surfactant interactions: Consequences for the amyloid-beta structure
Issue Date: 2012
Abstract: 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.
Subject: Ciências da Saúde, Ciências Tecnológicas, Ciências biológicas
Health sciences, Technological sciences, Biological sciences
Scientific areas: Ciências exactas e naturais::Ciências biológicas
Natural sciences::Biological sciences
URI: https://repositorio-aberto.up.pt/handle/10216/104617
Related Information: info:eu-repo/grantAgreement/FCT - Fundação para a Ciência e Tecnologia/Projectos de I&DT em Todos os Domínios Científicos/Referência: PTDC/QUI-BIQ/102827/2008/Concepção de péptidos fluorados para inibição da agregação do péptido beta-amilóide e avaliação da sua actividade biológica/Referência: PTDC/QUI-BIQ/102827/2008
Document Type: Artigo em Revista Científica Internacional
Rights: restrictedAccess
Appears in Collections:FEUP - Artigo em Revista Científica Internacional

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