Modulatory effects of pH, Cu+2 and sheet breakers on aggregation of amyloid peptides

Protein Pept Lett. 2005 Feb;12(2):197-202. doi: 10.2174/0929866053005845.

Abstract

The study explores in vitro by circular dichroism and mass spectrometry the effects of pH, Cu+2 ions and sheet-breakers on the secondary structures and self-aggregation of beta-amyloid peptides [Abeta43, Abeta42 and Abeta40] 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. beta-sheet breakers can reverse the self-aggregation process, suggesting their potential therapeutic use.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alzheimer Disease / metabolism
  • Alzheimer Disease / therapy
  • Amino Acid Sequence
  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / genetics
  • Amyloid beta-Peptides / metabolism
  • Circular Dichroism
  • Copper / chemistry*
  • Humans
  • Hydrogen-Ion Concentration*
  • Mass Spectrometry
  • Molecular Sequence Data
  • Peptide Fragments / chemistry*
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism
  • Protein Structure, Secondary*

Substances

  • Amyloid beta-Peptides
  • Peptide Fragments
  • Copper