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Additionally, tyrosines play an important role in aSyn-vesicle binding while nitration impairs this interaction (making the charge more negative at the N-terminal domain, or causing a conformational change when the C-terminal domain is nitrated) thereby increasing the amount of aSyn in a random coil or beta-sheet conformation and thus shifting equilibrium toward oligomer formation 105,106,109

We also evaluated in vivo biosafety and found no significant weight changes in any of the treatment groups during the experiment (Additional file 1: Fig