Inhibition of amyloid fibril formation of β-amyloid peptides via the amphiphilic surfactants
Resource
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1741 (3): 307-313
Journal
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
Journal Volume
1741
Journal Issue
3
Pages
307-313
Date Issued
2005
Date
2005
Author(s)
Abstract
β-amyloid peptide (Aβ) is the major proteinacious constituent of senile plaques in Alzheimer's disease and is believed to be responsible for the neurodegeneration process associated with the disease. While the actual size of the aggregated species responsible for Aβ neurotoxicity and fibrillogenesis mechanism(s) remain unknown, retardation of Aβ aggregation still holds assurance as an effective strategy in reducing Aβ-elicited toxicity. The research presented here is aimed at examining the inhibitory effect of two amphiphilic surfactants, di-C6-PC and di-C7-PC, on the in vitro fibrillogenesis process of Aβ(1-40) peptides at physiological pH (pH 7.2). Using ThT-induced fluorescence, turbidity, Congo red binding, and circular dichroism spectroscopy studies, our research demonstrated that the inhibition of Aβ(1-40) fibril formation was di-C6-PC and di-C7-PC concentration- dependent. The best inhibitory action on fibril formation was observed when Aβ was incubated with di-C7-PC at 100 μM over time. We believe that the outcome from this work will aid in the development and/or design of potential inhibitory agents against amyloid formation associated with Alzheimer's and other amyloid diseases. © 2005 Elsevier B.V. All rights reserved.
SDGs
Type
journal article
File(s)![Thumbnail Image]()
Loading...
Name
07.pdf
Size
379.6 KB
Format
Adobe PDF
Checksum
(MD5):22b7e7025f808f155fae7ad297a6343a