Complicated function of dopamine in A?-related neurotoxicity: Dual interactions with Tyr10 and SNK(26
By Mengmeng Liu and Lu Kou and Yannan Bin and Liping Wan and Juan Xiang
Published in Journal of Inorganic Biochemistry
2016
Abstract
With the capability to inhibit the formation of amyloid ? peptides (A?) fibril, dopamine (DA) and other catechol derivatives have been considered for the potential treatment of Alzheimer's disease (AD). Such treatment, however, remains debatable because of the diverse functions of A? and \DA\ in \AD\ pathology. Moreover, the complicated oxidation accompanying \DA\ has caused the majority of the previous research to focus on the binding of \DA\ oxides onto A?. The molecular mechanism by which A? interacts with the reduction state of DA, which is correlative with the brain function, should be urgently explored. By controlling rigorous anaerobic experimental conditions, this work investigated the molecular mechanism of the A?/DA interaction, and two binding sites were revealed. For the binding of DA, Tyrosine (Tyr10) was identified as the strong binding site, and serine-asparagine-lysing (SNK(26