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PM inhibition effect on α-synuclein (Syn) modification by dopamine (DA)
1. Syn was digested with three different enzymes, trypsin, V8, and chemotrypsin. Sequence coverage (%) of each enzyme was 72.9, 83.6, and 38.9, respectively. Sum of those enzymatic peptides covered 100% sequence of Syn, which is important to identify modification sites on Syn.
2. In the reaction of Syn with DA, multiple modifications on Syn were identified as follows: +dopamine quinone (DAQ), K43, 45, 96, 97, and 102; +DAQ-H2O, K21; oxidation, M1, 5, 116, and 127.
3. Met oxidation was increased in a DA dose-dependent manner. When Syn was incubated with DA in the presence of pyridoxamine (PM), a PM dose-dependent decrease in oxidation levels were observed for M116 and 127, located in C-terminal calcium binding domain.
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