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

被引：102

作者：

Rocha, Sandra ^{[1
]}

Thueneman, Andreas F. ^{[2
]}

Pereira, Maria do Carmo ^{[1
]}

Coelho, Manuel ^{[1
]}

Moehwald, Helmuth ^{[3
]}

Brezesinski, Gerald ^{[3
]}

机构：

[1] Univ Porto, Fac Engn, Dept Chem Engn, LEPAE, P-4200465 Oporto, Portugal

[2] Fed Inst Mat Res & Testing, D-12489 Berlin, Germany

[3] Max Planck Inst Colloids & Interfaces, D-14424 Potsdam, Germany

来源：

BIOPHYSICAL CHEMISTRY | 2008年 / 137卷 / 01期

关键词：

amyloid beta-peptide; circular dichroism; conformation analysis; electron microscopy; fluorinated complexes; nanoparticles;

D O I：

10.1016/j.bpc.2008.06.010

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (c) 2008 Elsevier B.V. All rights reserved.

引用

页码：35 / 42

页数：8

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