Date Approved

2006

Degree Type

Open Access Senior Honors Thesis

Department or School

Chemistry

Abstract

Abstract 1: α-Amylase is an important enzyme in the body responsible for hydrolyzing many polysaccharides such as dietary starch. Inhibition of this enzyme could be extremely beneficial in diabetic patients because it could lower the glucose levels in the blood. Our objective is to synthesize a small analog of a natural α-amylase inhibitor, Tendamistat. This molecule has 15-22 residue segment that are critical for its activity. The peptide was synthesized, cleaved, purified, analyzed, and an enzyme assay was run. Michaelis Menton and Lineweaver-Burk plots were constructed to determine the Vmax, Km, and Ki for each assay and determine the activity. It was determined that the assays yielded inconclusive data, and therefore, it could not be determined whether competitive inhibition was occurring. Also the Kis for the synthesized peptide and the native peptide were extremely different which also tells us that this is not going to be a useful drug for diabetic patients.

Abstract 2: The LL-21 is the smallest active sequence for the antimicrobial LL-37 peptide. Were LL-37 is a natural human immune defense and uses a different mechanism (drugs like penicillin which only attack bacteria during reproduction state) of entry into the bacterial cell wall. The research consisted of determining the activity of LL-21 against different bacterial strains. The methods to determine its activity were to synthesize, cleave, purify, and then send peptide to our U of M sponsor to analyze. The peptide was found to be active in the 0.4 to 100 μg/ml range. Further studies would use isotopically labeled groups on the peptide and be studied thoroughly by the NMR to find the mechanism of action.

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