Date of Award

5-2-2018

Degree Type

Thesis

Degree Name

Master of Science (MS)

Department

Chemistry

First Advisor

Irene Weber

Abstract

Human immunodeficiency virus (HIV) is a pandemic that has infected nearly 1% of the world population. Despite numerous FDA approved antiviral drugs, HIV drug resistance remains a large challenge. HIV protease is an enzyme that is required by the virus to cleave Gag and Gag-Pol polyproteins into functional and structural proteins necessary for viral maturation. Currently, nine clinical inhibitors target HIV protease, but multiple clinical viral strains have developed resistance to these drugs. Therefore, it is necessary to continue developing new drugs to tackle the problem of HIV drug resistance, and X-ray crystallography is one tool that is used to study how drug candidates bind to HIV-1 protease. In order to study the interactions between inhibitor atazanavir and HIV-1 protease, the crystal structure of the complex has been solved at atomic resolution (1.09 Å). This structure will improve the design of new inhibitors for resistant protease.

Available for download on Saturday, April 25, 2020

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