Substoichiometric inhibition of Aβ1-40 aggregation by a tandem Aβ40-1-Gly8-1-40 peptide

Sourajit M. Mustafi, Kanchan Garai, Scott L. Crick, Berevan Baban, Carl Frieden

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5 Scopus citations


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.

Original languageEnglish
Pages (from-to)509-512
Number of pages4
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Jul 2010


  • Atomic force microscopy
  • Fibrillization
  • Reverse sequence
  • ThioflavinT


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