【摘要】 α-突触核蛋白(α-synuclein,α-Syn)在体内异常折叠和纤维化是帕金森病(Parkinson′s disease,PD)发生发展的重要原因.DJ-1蛋白作为分子伴侣可以促进α-Syn的正常折叠,在PD中发挥着重要作用.利用大肠杆菌研究DJ-1的表达对-αSyn(A53T,S129A)折叠的影响.结果表明,野生型DJ-1(WT)使α-Syn(A53T)和α-Syn(S129A)正常折叠分别提高了48%和16%;而突变的DJ-1(M26I,R98Q)丧失了促进α-Syn(A53T)和α-Syn(S129A)正常折叠的功能.更多还原

【Abstract】 The abnormal folding and fibrosis of α-synuclein is a main reason in Parkinson’s disease.As a molecular chaperone,DJ-1 can increase the correct folding of α-synuclein(A53T,S129A)and plays an important role in Parkinson’s disease.In the experiment,we studied the ability of DJ-1 to increase correct folding of α-synuclein(A53T,S129A) in bacteria.The results showed that wild-type DJ-1 could increase the correct folding of α-synuclein(A53T) by 48% and α-synuclein(S129A) by 16%;whereas mutate DJ-1(M26I,R98Q) could not increase the correct folding α-synuclein(A53T,S129A).更多还原