Protein Misfolding Studies on Human Semenogelin-1 and Serum Albumin Proteins

Proper folding of proteins into native structure is essential for their biological activity. Proteins achieve native state with the help of several cellular regulatory mechanismsassisted by molecular chaperones. Alteration in these regulatory mechanisms can lead to protein misfolding. Also failure to dispose of the misfolded protein load causes accumulation of misfolded proteins and toxicity. The accumulated protein in some cases may self-assemble into stable, β-sheet rich oligomers and aggregates known as amyloid fibrils. Amyloid aggregation has been implicated to cause several diseases such as Alzheimer’s, Parkinson’s and \nrenal amyloidosis etc.