468048 Conformational Ensemble of Islet Amyloid Polypeptide in a Membrane Environment

Tuesday, November 15, 2016: 10:06 AM
Yosemite A (Hilton San Francisco Union Square)
Gregory L. Dignon, Chemical and Biomolecular Engineering, Lehigh University, Bethlehem, PA, Jeetain Mittal, Department of Chemical and Biomolecular Engineering, Lehigh University, Bethlehem, PA and Gül H. Zerze, Department of Chemical Engineering, Lehigh University, Bethlehem, PA

Islet Amyloid Polypeptide (IAPP) is a 37 residue intrinsically disordered protein implicated in the pathology of Type II Diabetes. Intrinsically disordered proteins have no definite structure, but rather sample an ensemble of structures. IAPP, also called Amylin, has been found to form amyloid fibrils due to misfolding and aggregation which is accelerated in the presence of lipid bilayers. When Amylin is in a membrane environment, its conformational ensemble is altered in ways which promote the formation of these amyloid fibrils. Using atomistic molecular dynamics simulations, we probe the conformational ensemble of Amylin in bulk, as well as in a membrane environment to observe the effects which cause the increased amyloidogenic activity.


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