Author

Brian Long

Date of Award

5-2018

Degree Type

Honors College Thesis

Department

Chemistry and Biochemistry

First Advisor

Douglas Masterson, Ph.D

Advisor Department

Chemistry and Biochemistry

Abstract

Pig Liver Esterase (PLE) is a serine protease enzyme that can interact with one side of a diester to hydrolyze the ester to a carboxylic acid, and research has found that the level of hydrophobicity of side groups can impact the enantioselectivity of PLE hydrolysis.1, 2 The Jones Model is what current researchers use to model the active site of PLE, but the nature of its binding pockets, namely the Hydrophobic Long (HL) pocket, has been called into question.3 Dimethyl 2-((pyrrole-2-yl)methyl)-2-methylmalonate was prepared to be subjected to PLE hydrolysis to see whether enantioselectivity was found. Chiral HPLC revealed 25.32% enantiomeric excess (e.e.) of the diester with the 2-position pyrrole side group. This proves that there are amino acid residues in the HL binding pocket that can interact with a hydrogen bond donor such as pyrrole and gives more credit to the questions of whether the hydrophobic binding pockets of PLE are really so hydrophobic.

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