Título: Journal of Peptide ScienceImportada do Authenticus Pesquisar Publicações da Revista

Vol. 19 Nº 9

Páginas: 581-587

ISSN: 1075-2617

Editora: Wiley-Blackwell

ISI Web of Knowledge - 14 Citações

Scopus - 16 Citações

FOS: Ciências exactas e naturais > Química

ID Authenticus: 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.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Contacto: mcsp@fe.up.pt

Nº de páginas: 7