Studies on Effect of Small Molecules on Protein Folding, Misfolding and Amyloidogenesis
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The correct folding of polypeptides to their native tertiary structure is a prerequisite for proper functioning of the proteins. However, despite several cellular quality control mechanisms, proteins sometimes gets misfolded and trapped as aggregates. The transition of proteins from their soluble, globular form to insoluble, fibrillar aggregates is one of the most elusive problems to modern science, which has been subjected to extensive research. These fibrillar aggregates sometimes exhibit highly stable and ordered structures which are known as ''amyloids''. Deposition of amyloids in the extracellular matrix has been the starting point of several degenerative diseases such as, AlzheimerDs disease, ParkinsonDs disease, Type II diabetes and so on. Currently, efforts are on to develope an efficient mode of therapy against amyloid diseases. The interesting property of amyloids of being highly similar in structural, toxicity, immunogenic and tinctorial properties, irrespective of their source proteins invite the attention towards development of a common mode of therapy..
Supervisor: V. K. Dubey
BIOSCIENCES AND BIOENGINEERING