Modulatory effects of pH, Cu+2 and sheet breakers on aggregation of amyloid peptides.
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.
Beking
Kris
K
Regional Protein Chemistry Center, Diseases of Aging Program, Ottawa Health Research Institute, 725 Parkdale Ave, Ottawa, ON. K1Y 4E9, Canada.
Hao
Xiaolei
X
Basak
Sarmistha
S
Basak
Ajoy
A
D000544:Alzheimer Disease / Q000378:metabolism / Q000628:therapy; D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D002942:Circular Dichroism; D003300:Copper / Q000737:chemistry*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017433:Protein Structure, Secondary
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; D003300:Copper