Date of Award
5-4-2022
Degree Type
Thesis
Degree Name
Master of Science (MS)
Department
Chemistry
First Advisor
Irene T. Weber
Second Advisor
Robert W. Harrison
Third Advisor
Hamed Laroui
Abstract
In 2020, 37.7 million individuals were living with HIV. If an individual infected with HIV does not undergo proper treatment, then the patient may obtain the disease acquired immunodeficiency syndrome. Although there are a myriad of HIV treatments and FDA-approved clinical inhibitors, drug resistance is the main obstacle to successful treatment plans. HIV protease is an essential protein that cleaves Gag and Gag-Pol polyproteins to yield infectious HIV. Due to HIV's rapid mutation, it is vital to develop more effective treatments and drugs for drug-resistant strains. X-ray crystallography and enzyme kinetics experiments are used to understand the binding of inhibitors to HIV proteases and aid the development of novel clinical inhibitors for resistant mutants of the protease. The binding of peptide analogs was studied for highly drug-resistant mutant PRS17 with a V48G mutation to wildtype residue. The revertant mutation showed small changes in inhibition or protease structure relative to PRS17.
DOI
https://doi.org/10.57709/28902458
Recommended Citation
Verhoff, Sarah R., "Enzyme Kinetics and Structural Studies of Drug Resistant HIV Protease." Thesis, Georgia State University, 2022.
doi: https://doi.org/10.57709/28902458
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