Abstract:
:α-Synuclein (α-Syn) oligomerization and amyloid formation are associated with Parkinson's disease (PD) pathogenesis. Studying familial α-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 α-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.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Ghosh D,Sahay S,Ranjan P,Salot S,Mohite GM,Singh PK,Dwivedi S,Carvalho E,Banerjee R,Kumar A,Maji SKdoi
10.1021/bi5010365subject
Has Abstractpub_date
2014-10-21 00:00:00pages
6419-21issue
41eissn
0006-2960issn
1520-4995journal_volume
53pub_type
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