Influence of fluorinated and hydrogenated nanoparticles on the structure and fibrillogenesis of amyloid beta-peptide

• Tipo: Artigo em Revista Científica Internacional
• Data: 2008

Autores

Sandra Rocha (Autor) Outra; Andreas F Thueneman (Autor) Outra; Maria do Carmo Pereira (Autor) FEUP; Manuel Coelho (Autor) FEUP; Helmuth Moehwald (Autor) Outra; Gerald Brezesinski (Autor) Outra

Revista

Título: Biophysical Chemistry

Vol. 137

Páginas: 35-42

ISSN: 0301-4622

Editora: Elsevier

Indexação

ISI Web of Knowledge - 87 Citações

Scopus - 51 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Química

Outras Informações

ID Authenticus: P-003-WCP

DOI: 10.1016/j.bpc.2008.06.010

Abstract (EN): Peptide aggregation in amyloid fibrils is implicated in the pathogenesis of several diseases such as Alzheimer's disease. There is a strong correlation between amyloid fibril formation and a decrease in conformational stability of the native state. Amyloid-P peptide (A beta), the aggregating peptide in Alzheimer's disease, is natively unfolded. The deposits found in Alzheimer's disease are composed of A beta fibrillar aggregates rich in beta-sheet structure. The influence of fluorinated complexes on the secondary structure and fibrillogenesis of A beta peptide was studied by circular dichroism, (CD) spectroscopy and transmission electron microscopy (TEM). CD spectra show that complexes of polyampholyte and fluorinated dodecanoic acid induce alpha-helix structure in A beta, but their hydrogenated analogous lead to beta-sheet formation and aggregation, The fluorinated nanoparticles with highly negative zeta potential and hydrophobic fluorinated core have the fundamental characteristics to prevent: A beta fibrillogenesis.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 8