Blocking Formation Of Toxic Plaques Implicated In Type 2 Diabetes

The report cites evidence correlating increases in amyloid formation in the pancreas with increases in severity and rate of progression of type-2 diabetes, which affects almost 20 million Americans and is rapidly rising worldwide.

Deposits of the abnormal protein damage and destroy insulin-producing "islet" cells in the pancreas. Researchers have been seeking potential new medicines that block formation of an abnormal, misfolded protein called islet amyloid polypeptide (IAPP), which may play a key role in the cell destruction.

In the new study, Daniel Raleigh, Andisheh Abedini and Fangli Meng found that changing a single amino acid in human IAPP's structure transformed it from one of the most potent amyloid-forming substances into a powerful inhibitor of amyloid formation. In laboratory studies, they showed that the mutant IAPP significantly reduced the amount of amyloid formed. In addition to opening the door for better IAPP inhibitors in type-2 diabetes, the findings provide potentially important insights into the formation and treatment of amyloid plaques in Alzheimer's disease, Parkinson's disease, and other conditions, the researchers say.

Article: "A Single-Point Mutation Converts the Highly Amyloidogenic Human Islet Amyloid Polypeptide into a Potent Fibrillization Inhibitor" Journal of the American Chemical Society, September 5, 2007