Date of Completion


Degree Type

Honors Thesis - Campus Access


Chemistry (CHEM)

First Advisor

David A. Moffet, Ph.D.


Islet Amyloid Polypeptide (IAPP) is a 37-amino acid polypeptide that is known to misfold and aggregate into toxic oligomers and fibrils. These amyloid aggregates have been linked to the death of insulin-secreting pancreatic β-islet cells and contribute to the development of type II diabetes. New developments in therapeutics can come from inhibiting the aggregation of IAPP. The extracts of 14 vegetables and 5 teas were screened for their ability to inhibit the toxic aggregation of IAPP, knowing that vegetables and teas have a multitude of possible health effects. The antiamyloid ability of these extracts were tested by using thioflavin T assays, visualizing amyloid fibrils with atomic force microscopy (AFM), and performing MTT assays. From all of these screening methods, one vegetable extract and one tea extract appeared to demonstrate therapeutic potential to inhibit aggregation of IAPP.