| Literature DB >> 20515649 |
Sourajit M Mustafi1, Kanchan Garai, Scott L Crick, Berevan Baban, Carl Frieden.
Abstract
Abeta peptides aggregate to form insoluble and neurotoxic fibrils associated with Alzheimer's disease. Inhibition of the aggregation has been the subject of numerous studies. Here we describe a novel, substoichiometric inhibitor of Abeta(1-40) fibrillization as a tandem dimeric construct consisting of Abeta(40-1) (reverse sequence) linked to Abeta(1-40) via an eight residue glycine linker. At molar ratios of the tandem peptide to Abeta(1-40) of 1:10 to 1:25 inhibition of fibrillization, as measured by ThioflavinT, was observed. We postulate that the tandem construct binds to a fibrillar intermediate but the reverse sequence delays or prevents further monomer association. Copyright 2010 Elsevier Inc. All rights reserved.Entities:
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Year: 2010 PMID: 20515649 PMCID: PMC2897963 DOI: 10.1016/j.bbrc.2010.05.144
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575