Pyridine-appended Bis-functionalized 1,2,3 Triazoles as Inhibitors of Protein Tyrosine Phosphatases
Faculty Mentor
Shainaz Landge
Location
Russell Union Ballroom
Type of Research
On-going
Session Format
Poster Presentation
College
College of Science & Mathematics
Department
Biochemistry, Chemistry, and Physics
Abstract
Protein Tyrosine Phosphatases (PTP) play a critical role in bacteria’s ability to infect a host. Consequently, PTP inhibitors have recently been investigated for their antibacterial ability. A series of novel 1,2,3-triazole derivatives were synthesized via copper-catalyzed azide-alkyne cycloaddition (CuAAC) and were characterized using nuclear magnetic resonance (NMR) spectroscopy, infrared (IR) spectroscopy, melting point analysis, and high-resolution mass spectrometry (HRMS). In silico molecular docking studies were conducted to predict binding affinities and interaction profiles of the compounds with the protein tyrosine phosphatase target. Subsequent in vitro enzyme inhibition assays were performed to assess biological activity and validate computational predictions. These characterizations provided a prediction for the pharmacokinetics of the synthesized compounds, including binding and drug bioavailability in a biological environment. This goal of this research is to find a compound capable of inhibiting protein tyrosine phosphatase (PTP) activity. This is significant because (PTP) activity is vital for bacterial function and pathogenicity. If we are successful, we will have synthesized a compound that can kill bacteria by inhibiting their ability to successfully infect a host.
Program Description
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Start Date
4-23-2026 2:00 PM
End Date
4-23-2026 4:00 PM
Recommended Citation
Westervelt, Scott E.; Landge, Shainaz Dr.; Dela Cerna, Mark Vincent; and Bennett, Grace M., "Pyridine-appended Bis-functionalized 1,2,3 Triazoles as Inhibitors of Protein Tyrosine Phosphatases" (2026). GS4 Student Scholars Symposium. 213.
https://digitalcommons.georgiasouthern.edu/research_symposium/2026/2026/213
Pyridine-appended Bis-functionalized 1,2,3 Triazoles as Inhibitors of Protein Tyrosine Phosphatases
Russell Union Ballroom
Protein Tyrosine Phosphatases (PTP) play a critical role in bacteria’s ability to infect a host. Consequently, PTP inhibitors have recently been investigated for their antibacterial ability. A series of novel 1,2,3-triazole derivatives were synthesized via copper-catalyzed azide-alkyne cycloaddition (CuAAC) and were characterized using nuclear magnetic resonance (NMR) spectroscopy, infrared (IR) spectroscopy, melting point analysis, and high-resolution mass spectrometry (HRMS). In silico molecular docking studies were conducted to predict binding affinities and interaction profiles of the compounds with the protein tyrosine phosphatase target. Subsequent in vitro enzyme inhibition assays were performed to assess biological activity and validate computational predictions. These characterizations provided a prediction for the pharmacokinetics of the synthesized compounds, including binding and drug bioavailability in a biological environment. This goal of this research is to find a compound capable of inhibiting protein tyrosine phosphatase (PTP) activity. This is significant because (PTP) activity is vital for bacterial function and pathogenicity. If we are successful, we will have synthesized a compound that can kill bacteria by inhibiting their ability to successfully infect a host.
