Computational Biology
Kyle Hoffman
Department of Chemical and Biological Engineering
UW-Madison
1/31/12
The Interaction of Islet Amyloid Polypeptide with Phospholipid Bilayers and
Micelles
Tuesday
4:00 pm
Biotechnology Center Auditorium, 425 Henry Mall
Abstract:
    The aggregation of the 37 residue polypeptide human amylin is strongly
linked to the development of Type II Diabetes. The human and rat sequences
of the peptide differ by only 6 residues; however, the human version
aggregates into fibrils while the rat version does not. While the
conformations these proteins adopt in solution have been studied
extensively, their structures in the presence of lipid bilayers where the
aggregation process is substantially accelerated are unknown. By studying
the differences between the structures, insight into the aggregation process
can be gained. Using molecular dynamics and other advanced sampling
techniques, we show that the structure of human and rat amylin near a lipid
bilayer are a random coil. However, in the presence of a micelle, the rat
amylin adopts a more α-helical conformation. These structures will allow us
to begin studying the aggregation process in the presence of membranes.