Date of Award

6-7-2015

Document Type

Thesis - SCU Access Only

Publisher

Santa Clara University

First Advisor

Zhiwen Zhang

Abstract

Designing the ideal drug involves addressing certain key factors which include safety, specificity, solubility, and affinity. Protein drugs have gained momentum in the pharmacological field due to their abilities for high specificity and affinity for their target and low occurrences for drug-drug interactions. However, protein drugs are large molecules and their large molecular weight causes a more difficult time being transported across membranes in the body. In this paper, we used the method of reverse protein engineering with the technique of integrating a DNA library to shorten the amino acid sequence of the protein lipoprotein-associated phospholipase A2 (Lp-PLA2) in order to decrease its final size. Our experiments showed that a majority of the potential peptide candidates were negative for function and do not hydrolyze lipids, but more testing and sequencing must be done to determine the functionality of the inconclusive colonies. Furthermore, a different size of core region from Lp-PLA2 could be selected and tested.

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