Weekly Chemistry Seminar-Lauren Buchanan, University of Wisconsin-Madison
- 2/15/2013 |
3:00 PM – 4:00 PM
Location: Druckenmiller Hall, Room 020
Event Type: Seminar
Amyloid fiber formation is associated with more than twenty diseases, including type 2 diabetes and Alzheimer's disease. Thus, there is great interest in developing amyloid inhibitors as potential therapeutics, but rational drug design is hindered by the dearth of detailed information about the structure and aggregation mechanism of amyloid fibers. Our group uses 2D IR spectroscopy with isotope labeling to study amyloid peptides and drug binding with residue-level structural specificity. I will introduce the method behind our spectroscopic technique and show how it has been applied to study hIAPP, the peptide implicated in type-II diabetes. Our results provide significant insight into the aggregation mechanism of hIAPP and experiments with a novel macrocyclic peptide inhibitor suggest a new approach to designing amyloid inhibitors.