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αSynuclein (AS) is an intrinsically disordered protein that can misfold and aggregate to form Lewy bodies in dopaminergic neurons, a classic hallmark of Parkinson's disease. The binding of Cu(II) and dopamine to AS was evaluated by nanopore analysis with αhemolysin. In the absence of Cu(II), wildtype AS (1 μm) readily translocated through the pore with a blockade current of − 85 pA, but mostly bumping events were observed in the presence of 25 μm Cu(II). A binding site in the Nterminus was confirmed, because Cu(II) had no effect on the event profile of a peptide consisting of the Cterminal 96–140 residues. In the presence of dopamine (25 μm), the translocation events at − 85 pA shifted to − 80 pA, which also represents translocation events, because the event time decreases with increasing voltage. Events at − 80 pA were also observed for the mutant A30P AS in the presence of dopamine. Event profiles …