Date Approved

2005

Degree Type

Open Access Senior Honors Thesis

Department

Chemistry

Abstract

Small analogues of Tendamistat, a natural protein inhibitor of mammalian α-amylase, were designed - the most effective of which was entitled NFH-l. Alanine and threonine substitutions were made separately for the third and seventh position serine residues to explore required properties of the NFH-l analogue and also in attempt to improve the inhibitory activity of the analogue. Substituted analogues were tested for inhibitory activity via color spectrophotometric assay and the threonine substituted analogues also explored through theoretical modeling. Through alanine substitution, it was found that the hydrogen bonding ability of both serine residues are integral to the function of the NFH -1 peptide. Through threonine substitutions and modeling, it was found that substitution into the seventh position alters conformation and not activity and substitution into the third position alters activity and not conformation.

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