Cytotoxicity of Aft with redox active metals in neuronal cells has been implicated in the progression of Alzheimer＇s disease （AD）. Zn7MT-3 protects cell against AβCu2＋ toxicity. The roles of single domain protei...Cytotoxicity of Aft with redox active metals in neuronal cells has been implicated in the progression of Alzheimer＇s disease （AD）. Zn7MT-3 protects cell against AβCu2＋ toxicity. The roles of single domain proteins （α/β） and α-β domain-domain interaction of ZnTMT-3 in its anti-Aβ1-42-Cu2＋ toxicity activity were investigated herein. Aβ1-42 and four mutants of human MT3 （α/β domain, β（MT3）--α（MT1） and △31-34） were prepared and characterized. Aβ1-42-Cu2＋ induced hydroxyl radical and ROS production with/without Zn-MTs were measured by fluorescence spectroscopy and DCFH-DA in living cells, respectively. These results indicate that the two domains form a co-operative unit and each of them is indispensable in conducting its bioactivity.展开更多
基金supported partly by the National Natural Science Foundation of ChinaShanghai Leading Academic Discipline Project(NoB108)PhD program of the Education Ministry of China(No20100071110011)
文摘Cytotoxicity of Aft with redox active metals in neuronal cells has been implicated in the progression of Alzheimer＇s disease （AD）. Zn7MT-3 protects cell against AβCu2＋ toxicity. The roles of single domain proteins （α/β） and α-β domain-domain interaction of ZnTMT-3 in its anti-Aβ1-42-Cu2＋ toxicity activity were investigated herein. Aβ1-42 and four mutants of human MT3 （α/β domain, β（MT3）--α（MT1） and △31-34） were prepared and characterized. Aβ1-42-Cu2＋ induced hydroxyl radical and ROS production with/without Zn-MTs were measured by fluorescence spectroscopy and DCFH-DA in living cells, respectively. These results indicate that the two domains form a co-operative unit and each of them is indispensable in conducting its bioactivity.
