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

• Type: Article in International Scientific Journal
• Date: 2008

Authors

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

Journal

Title: Biophysical Chemistry

Vol. 137

Pages: 35-42

ISSN: 0301-4622

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 87 Citations

Scopus - 51 Citations

Scientific classification

FOS: Natural sciences > Chemical sciences

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 8