Modulatory Effects of pH, Cu+2 and Sheet Breakers on Aggregation of Amyloid Peptides

Author(s): Kris Beking, Xiaolei Hao, Sarmistha Basak, Ajoy Basak

Journal Name: Protein & Peptide Letters

Volume 12 , Issue 2 , 2005

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The study explores in vitro by circular dichroism and mass spectrometry the effects of pH, Cu+2 ions and sheetbreakers on the secondary structures and self-aggregation of b-amyloid peptides [Aβ43, Aβ42 and Ab40] of Alzheimers disease. Within pH 5.4-7.3, more sheet structures and aggregates containing up to 11 peptide units were observed. Cu+2 ions led to oxidative degradation or aggregation depending on its concentration and time of incubation. β-sheet breakers can reverse the self-aggregation process, suggesting their potential therapeutic use.

Keywords: amyloid peptides, protein aggregation, secondary structure, sheet breakers, copper ions, ph, circular dichroism, mass spectrometry

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Article Details

Year: 2005
Page: [197 - 202]
Pages: 6
DOI: 10.2174/0929866053005845
Price: $65

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