Effect of polyols on the structure and aggregation of recombinant human γ-Synuclein, an intrinsically disordered protein

Biochimica Et Biophysica Acta. Proteins and Proteomics
Sneha Roy, Rajiv Bhat

Abstract

Polyol osmolytes accumulated in cells under stress are known to promote stability in globular proteins with respect to their increasing hydroxyl groups but their effect on the structure, stability and aggregation of intrinsically disordered proteins (IDPs) is still elusive. The lack of a natively folded structure in intrinsically disordered proteins under physiological conditions results in their aggregation and fibrillation that gives rise to a number of diseases. We have investigated the effect of a series of polyols, ethylene glycol (EG), glycerol, erythritol, xylitol and sorbitol on the fibrillation pathway of recombinant human γ-Synuclein, used as a model, for an IDP known to form fibrils that play a role in neurodegeneration and cancer. With an increase in the number of -OH groups in polyols except EG, we observe a decrease in lag time for fibrillation at equimolar concentrations, suggesting stronger preferential exclusion of polyols that promotes γ-Syn self-association and oligomerization. The polyols act early during nucleation and their diverse effect on the rate of fibrillation suggests the role of favourable solvent-side chain interactions. With increasing -OH group, polyols stabilize the natively unfolded conformati...Continue Reading

Citations

May 4, 2021·Langmuir : the ACS Journal of Surfaces and Colloids·Yu LiuJianyuan Hao

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