The formation of highly structured protein aggregates known as amyloid fibrils has been tied to over 20 different diseases, including type II diabetes, rheumatoid arthritis, Alzheimer’s disease, and Parkinson’s diseases. In each case, a normally soluble protein undergoes a radical conformation change that eventually leads to the formation of the toxic amyloid fibrils. In our work, formation of fibrils from insulin and bovine serum albumin were monitored using spectroscopic techniques and atomic force microscopy. Samples were incubated both in the presence and absence of different polyphenolic acids. The presence of the polyphenols was found to slow down the formation of amyloid fibrils. Examination of the fibrils by atomic force microscopy found that the fibrils incubated with the polyphenols were much shorter and rougher than fibrils formed in their absence, though the polyphenols were not able to break down the structure of already formed fibrils. The ability of the polyphenols to inhibit amyloid formation suggests a possible therapeutic approach to the treatment of amyloid diseases.

Effects of polyphenolic acids on amyloid formation

251st National Meeting (2016)

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