Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1952174 | Biochimie | 2013 | 4 Pages |
Abstract
We have studied the effect of a series of stabilizing and destabilizing osmolytes on the fibrillation pattern of a model amyloidogenic protein, HypF-N. Under mildly denaturing conditions, HypF-N forms cross β-sheet structures, characteristic of amyloid fibrils. In the presence of all stabilizing osmolytes except proline, fibrillation of HypF-N is inhibited. Notably, fibrillation kinetics is retarded at subdenaturing concentrations of chaotropes. In case of proline, fibrillation of HypF-N is accelerated. Thus, the changes during exposure of a protein to denaturing conditions in the presence of osmolyes cannot be extrapolated from their role as anti-fibrillation agents.
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Authors
Rupen D. Bhavsar, Shivcharan Prasad, Ipsita Roy,