Abstract
The misfolding and aggregation of intrinsically disordered proteins (IDPs) are believed to play crucial roles in developing neurodegenerative diseases, such as AD and PD. Nevertheless, the roles of metal ions and lipid membranes in IDPs aggregation are not fully understood. We investigated the interactions of amyloid-β (Aβ) peptide and α-synuclein with metal ions and lipid membranes using a variety of fluorescence spectroscopic tools including single molecule approaches. Stopped-flow fluorescence spectroscopy was used to study the kinetics of binding between these two IDPs and Cu2+.
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