GS4 Student Scholars Symposium

Aberrant protein tyrosine phosphatase (PTP) activity is implicated in a variety of diseases including obesity, type II diabetes, and cancer, among others. As the burden these diseases place on healthcare systems continues to grow, the development of novel therapeutics is more important than ever. 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-e) were synthesized using copper (I)-catalyzed, microwave-assisted click reaction. Compound characterization was performed using 1H NMR, 13C NMR, 19F NMR (where applicable), IR, and MS. The compounds were screened for inhibitory activity against PTP1b & PRL3 in fluorogenic substrate assays containing DiFMUP. Molecular docking analysis was conducted to evaluate bonding affinity of reported compounds.