Charged surfactants induce a non-fibrillar aggregation pathway of amyloid-beta peptide

• Type: Article in International Scientific Journal
• Date: 2013

Authors

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

Journal

Title: Journal of Peptide Science

Vol. 19 No. 9

Pages: 581-587

ISSN: 1075-2617

Publisher: Wiley-Blackwell

Indexing

ISI Web of Knowledge - 14 Citations

Scopus - 16 Citations

Scientific classification

FOS: Natural sciences > Chemical 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

PTDC/QUI-BIQ/118076/2010 - Liposomas funcionalizados com anticorpos para a doença de Alzheimer

BIONANO - Distibuição de biomoleculas através de nanopartículas inorganica/organicas

Other information

Authenticus ID: P-006-7YR

DOI: 10.1002/psc.2535

Abstract (EN): The amyloid -peptide with a sequence of 42 amino acids is the major constituent of extracellular amyloid deposits in Alzheimer's disease plaques. The control of the peptide self-assembly is difficult to achieve because the process is fast and is affected by many variables. In this paper, we describe the effect of different charged and non-charged surfactants on A((1-42)) fibrillation to define common alternate aggregation pathways. The characterization of the peptide-surfactant interactions by ultra-structural analysis, thioflavin T assay and secondary structure analysis, suggested that charged surfactants interact with A((1-42)) through electrostatic interactions. Charged micelles slow down the aggregation process and stabilize the peptide in the oligomeric state, whereas non-charged surfactants promote the A((1-42)) fibril formation. Copyright (c) 2013 European Peptide Society and John Wiley & Sons, Ltd.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 7