Abstract
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
Protein & Peptide Letters
Title: Modulatory Effects of pH, Cu+2 and Sheet Breakers on Aggregation of Amyloid Peptides
Volume: 12 Issue: 2
Author(s): Kris Beking, Xiaolei Hao, Sarmistha Basak and Ajoy Basak
Affiliation:
Keywords: amyloid peptides, protein aggregation, secondary structure, sheet breakers, copper ions, ph, circular dichroism, mass spectrometry
Abstract: 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.
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Cite this article as:
Beking Kris, Hao Xiaolei, Basak Sarmistha and Basak Ajoy, Modulatory Effects of pH, Cu+2 and Sheet Breakers on Aggregation of Amyloid Peptides, Protein & Peptide Letters 2005; 12 (2) . https://dx.doi.org/10.2174/0929866053005845
DOI https://dx.doi.org/10.2174/0929866053005845 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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