Date Approved

2007

Degree Type

Open Access Senior Honors Thesis

Department

Chemistry

First Advisor

Dr. Deborah Heyl-Clegg

Second Advisor

Dr. Heather Holmes

Abstract

α-Amylase is an enzyme that breaks down polysaccharides into their glucose subunits. It is one of the enzymes important in controlling blood sugar levels in the body. Inhibiting α-amylase could be a beneficial treatment for insulin-dependent diabetes mellitus, obesity, and hyperlipaemia. Naturally occurring Tendamistat has been found with such inhibitory affects, but there are drawbacks to this molecule and a small variation was synthesized. Several variations of the parent were tested in this research, exchanging Tyr15 for other residues to test for how a pKa change affects the inhibitory property. The peptide sequences were synthesized, cleaved, and purified through High Performance Liquid Chromatography before conducting three assays on each that varied in the concentration of inhibitor used. The rates of the reactions were then analyzed using Michealis-Menten and Lineweaver-Burk plots to conclude an average Ki value. In general, as the pKa value for the modification to the parent compound increased, the Ki values also increased, suggesting an importance of hydrogen bonding between the inhibitor and the enzyme.

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