Generic placeholder image

Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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

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

Volume 12, Issue 2, 2005

Page: [197 - 202] Pages: 6

DOI: 10.2174/0929866053005845

Price: $65

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


Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy