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://hdl.handle.net/10216/104617 |
Related Information: | info:eu-repo/grantAgreement/FCT - Fundação para a Ciência e a 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 |
Files in This Item:
File | Description | Size | Format | |
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65242.pdf Restricted Access | Artigo original publicado | 738.37 kB | Adobe PDF | Request a copy from the Author(s) |
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