Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1931901 | Biochemical and Biophysical Research Communications | 2010 | 4 Pages |
Abstract
Aβ 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 Aβ1-40 fibrillization as a tandem dimeric construct consisting of Aβ40-1 (reverse sequence) linked to Aβ1-40 via an eight residue glycine linker. At molar ratios of the tandem peptide to Aβ1-40 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.
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Authors
Sourajit M. Mustafi, Kanchan Garai, Scott L. Crick, Berevan Baban, Carl Frieden,