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

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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 Alzheimer's 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; circular dichroism; copper ions; mass spectrometry; ph; protein aggregation; secondary structure; sheet breakers

Document Type: Review Article


Affiliations: Regional Protein Chemistry Center, Diseases of Aging Program, Ottawa Health Research Institute, 725 Parkdale Ave, Ottawa, ON. K1Y 4E9, Canada.

Publication date: 2005-02-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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