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Effect of structural heterogeneity of α-synuclein mutants on the Aggregation propensity

Author: 
Airy Sanjeev and Venkata Satish Kumar Mattaparthi
Subject Area: 
Life Sciences
Abstract: 

Parkinson's disease is related to the aggregation of α-synuclein but the effect of single-point mutations (A53T, E46K and A30P) on the early events of aggregation remains elusive. The effect of structural heterogeneity of α-synuclein mutants in promoting the dimerization is critical. From the conformational dynamics of monomers of α-synuclein (WT and mutants), we noticed mutants to display beta structures and more intra-molecular contacts. We also studied inter-molecular interactions promoting the dimerization. We observed lesser number of inter-molecular interactions in the homo-dimer of WT than the mutants. The interactions demonstrated here may be used to design potential inhibitors to inhibit dimerization.

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