Document Type

Dissertation

Date of Award

12-2023

School/College

College of Pharmacy and Health Sciences (COPHS)

Degree Name

Ph.D. in Pharmaceutical Science

Committee Chairperson

Selvam Chelliah

Committee Member 1

Shirlette Milton

Committee Member 2

Katsuri Ranganna

Committee Member 3

Hector Miranda

Keywords

cancer, DNA repair, PARP1, structure-based drug design

Abstract

In the United States of America alone, cancer is the second highest cause of death. While there have been many remarkable breakthroughs in cancer research, there is still a need for the development of new therapies that target the different mechanisms of cancer cells. Therefore, the focus of our research is identifying novel hit molecules targeting Poly (ADP-ribose) polymerase 1. Poly (ADP-ribose) polymerase 1 (PARP1) is an enzyme that has many distinct functions in the body. PARP1 has four domains: zinc fingers also known as the DNA binding domain, BRCT domain, WGR domain, and the ART catalytic domain. Its most notable function is in DNA repair, which is possible because of its DNA binding domain. PARP1 helps catalyze the DNA repair pathway of single-strand breaks. Some of the deadliest cancers upregulate Poly (ADP-ribose) polymerase 1 to escape cell death, making it a suitable target for drug discovery. This study uses a combination of virtual high throughput screening, structure-based drug design, molecular dynamics, and inhibitor screening to identify molecules targeting Poly (ADP-ribose) polymerase 1. Herein we discovered Hit 10, Hit 17, Hit 22, and Hit 24 in our PARP1 inhibitory screening and Hit 2, Hit 8, Hit 13, Hit 18, and Hit 22 from our molecular dynamics study, and Hit 22 showed good results in molecular dynamics and in screening with the PARP1 colorimetric kit with an IC50 value of 1.476 at 50 µM. It also has a novel structure that has never been reported for PARP1 inhibition. Based on our findings, Hit 22 could be a viable candidate for hit-to-lead characterization and could be evaluated further as a PARP1 inhibitor.

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