Date of Award


Degree Type

Open Access Thesis



Committee Member

Deborah Heyl-Clegg, Ph.D.

Committee Member

Hedeel Evans, Ph.D.


Polypeptide aggregation is seen in a variety of diseases (termed amyloidoses) but remains poorly understood. This study uses the polypeptide amylin to investigate how nonspecific interactions between peptides can inhibit aggregation. A set of 5 heptapeptides was assessed for its ability to impact amylin-induced membrane damage and aggregation. Solvent effects precluded accurate assessment of the impact on membrane damage; however a method of subtracting out the solvent effect is offered. The two most hydrophobic compounds showed the ability to substantially slow amylin aggregation, while those compounds carrying charged side chains tended to increase the rate of aggregation. Only one compound showed a concentration-dependent effect, which is offered as evidence for specific interactions. This study demonstrates that even random peptide sequences can have a significant impact on the behavior of an aggregating species, via specific and nonspecific associations.


Posted: 04-09-2013

Included in

Chemistry Commons