The Newly Discovered Parkinson鈥檚 Disease Associated Finnish Mutation (A53E) Attenuates 伪-Synuclein Aggregation and Membrane Binding

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• 作者：Dhiman Ghosh ; Shruti Sahay ; Priyatosh Ranjan ; Shimul Salot ; Ganesh M. Mohite ; Pradeep K. Singh ; Saumya Dwivedi ; Edmund Carvalho ; Rinti Banerjee ; Ashutosh Kumar ; Samir K. Maji
• 刊名：Biochemistry
• 出版年：2014
• 出版时间：October 21, 2014
• 年：2014
• 卷：53
• 期：41
• 页码：6419-6421
• 全文大小：232K
• ISSN：1520-4995

文摘

伪-Synuclein (伪-Syn) oligomerization and amyloid formation are associated with Parkinson鈥檚 disease (PD) pathogenesis. Studying familial 伪-Syn mutants associated with early onset PD has therapeutic importance. Here we report the aggregation kinetics and other biophysical properties of a newly discovered PD associated Finnish mutation (A53E). Our in vitro study demonstrated that A53E attenuated 伪-Syn aggregation and amyloid formation without altering the major secondary structure and initial oligomerization tendency. Further, A53E showed reduced membrane binding affinity compared to A53T and WT. The present study would help to delineate the role of A53E mutation in early onset PD pathogenesis.