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
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