Targeting Binding Site 1 of PRL3, an Oncogenic and Metastatic Phosphates, Through High-Throughput Screening
Faculty Mentor
Dr. Mark Vincent Dela Cerna
Location
Savannah Ballroom
Type of Research
On-going
Session Format
Poster Presentation
College
College of Science & Mathematics
Department
Biochemistry
Abstract
Authors: Hannah Scroggins, Mingyu Wang, Grace M. Bennett, Mark V.C. dela Cerna
Across cultures, cancer continues to claim lives as a primary cause of mortality. Specifically, cancer that has metastasized is directly connected with poor patient prognosis. Recent studies have indicated that in metastatic cancer lesions, a specific protein was overexpressed as opposed to normal tissue. That protein, phosphatase of regenerating liver 3 (PRL3), is the target protein in this project. PRL3 plays a significant role in oncogenic and metastatic pathways, validating our interest in investigating drugs that interfere with aggressive cancer cells. In pursuit of discovering molecules that may bind or inhibit PRL3, a high through-put virtual screening targeted a pocket that was previously identified through molecular dynamics simulations and computational pocket analysis. This virtual screening uses a library of over 3 million lead-like molecules. This library was obtained from ZINC15, filtered by availability (in-stock), molecular weight (300-350 Da), and solubility (-1.0 to 3.5 logP). From the filtered results, 4 molecules were chosen and purchased based on their predicted binding and/or inhibiting affinity. The predicted inhibition was tested of these molecules through the use of a multi-mode microplate reader, which detects chemical reactions through measuring fluorescence. After analysis of the initial screening, the molecules showed promising results of inhibiting the phosphatase activity of PRL3. To advance the testing of these molecules, dose dependence assays will be performed to determine IC50s. Eventually, the most promising molecules will move on to binding studies, including protein-based nuclear magnetic resonance (NMR) and isothermal titration calorimetry (ITC) where the reaction between PRL3 and these molecules will be determined.
Program Description
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Start Date
4-21-2026 10:00 AM
End Date
4-21-2026 12:00 PM
Recommended Citation
Scroggins, Hannah, "Targeting Binding Site 1 of PRL3, an Oncogenic and Metastatic Phosphates, Through High-Throughput Screening" (2026). GS4 Student Scholars Symposium. 30.
https://digitalcommons.georgiasouthern.edu/research_symposium/2026A/2026A/30
Targeting Binding Site 1 of PRL3, an Oncogenic and Metastatic Phosphates, Through High-Throughput Screening
Savannah Ballroom
Authors: Hannah Scroggins, Mingyu Wang, Grace M. Bennett, Mark V.C. dela Cerna
Across cultures, cancer continues to claim lives as a primary cause of mortality. Specifically, cancer that has metastasized is directly connected with poor patient prognosis. Recent studies have indicated that in metastatic cancer lesions, a specific protein was overexpressed as opposed to normal tissue. That protein, phosphatase of regenerating liver 3 (PRL3), is the target protein in this project. PRL3 plays a significant role in oncogenic and metastatic pathways, validating our interest in investigating drugs that interfere with aggressive cancer cells. In pursuit of discovering molecules that may bind or inhibit PRL3, a high through-put virtual screening targeted a pocket that was previously identified through molecular dynamics simulations and computational pocket analysis. This virtual screening uses a library of over 3 million lead-like molecules. This library was obtained from ZINC15, filtered by availability (in-stock), molecular weight (300-350 Da), and solubility (-1.0 to 3.5 logP). From the filtered results, 4 molecules were chosen and purchased based on their predicted binding and/or inhibiting affinity. The predicted inhibition was tested of these molecules through the use of a multi-mode microplate reader, which detects chemical reactions through measuring fluorescence. After analysis of the initial screening, the molecules showed promising results of inhibiting the phosphatase activity of PRL3. To advance the testing of these molecules, dose dependence assays will be performed to determine IC50s. Eventually, the most promising molecules will move on to binding studies, including protein-based nuclear magnetic resonance (NMR) and isothermal titration calorimetry (ITC) where the reaction between PRL3 and these molecules will be determined.
