Date of Completion


Degree Type

Honors Thesis - Campus Access


Chemistry (CHEM)

First Advisor

David A. Moffet, Ph.D.


The aggregation of Islet Amyloid Polypeptide (IAPP, amylin), a 37-amino acid polypeptide, has been thought to correlate with the loss of pancreatic β-islet cells that are necessary for the secretion of insulin. These effects appear to contribute to type II diabetes, and for this reason, the inhibition of the aggregate proteins can be vital for the discovery of potential therapeutic drugs. With the use of Thioflavin T binding assays, extracts of 14 vegetables and 5 teas were tested and analyzed for their in vitro abilities to inhibit the aggregation of amyloidogenic IAPP. Atomic force microscopy was used for samples of vegetable and tea extracts to visualize amyloid fiber formation and these results were compared to the amyloid fiber formation of IAPP alone. Additionally, the ability of the extracts to protect living mammalian cells from the toxic effects of IAPP was tested using HeLa cells. One vegetable and one tea demonstrated ability to both inhibit IAPP aggregation and protect living cells.