PRL3 and PTP1B Inhibition and Screening of Ortho-substituted 1,2,3-triazoles

Name

Asher D. Pence, Georgia Southern UniversityFollow

Publication Date

2025

Major

Biology (B.S.B.)

Release Option

Restricted to Georgia Southern

Faculty Mentor

Shainaz Landge

Abstract

Aberrant protein tyrosine phosphatase (PTP) activity is implicated in a variety of diseases including obesity, type II diabetes, Alzheimer’s disease, and cancer, among others. As the burden these diseases place on healthcare systems globally continues to grow, the development of novel therapeutic approaches is more important than ever to combat them. Protein tyrosine phosphatase 1b (PTP1b) and phosphatase of regenerating liver 3 (PRL3), two protein tyrosine phosphatases (PTPs) whose roles in the aforementioned diseases are well documented, have been widely identified as important targets for the development of novel treatments for these diseases. For this project, a set of ortho-substituted 1,2,3-triazoles (A-I) were synthesized using copper (I)-catalyzed, microwave-assisted click reaction. Compound characterization was performed using ¹H NMR, ¹³C NMR, ¹⁹FNMR (where applicable), IR, and HRMS. Molecular docking analysis was conducted to evaluate bonding affinity of reported compounds. The reported set of compounds were assayed with PRL3 and PTP1B to assess inhibitory activity.

Recommended Citation

Pence, Asher D., "PRL3 and PTP1B Inhibition and Screening of Ortho-substituted 1,2,3-triazoles" (2025). Honors College Theses. 1044.
https://digitalcommons.georgiasouthern.edu/honors-theses/1044