Green Synthesis of 3,4,6-Trisubstituted Pyridazines and Their Biological Evaluation Against PTP-1B
Faculty Mentor
Shainaz Landge
Location
Russell Union 2075
Type of Research
Completed
Session Format
Oral Presentation
College
College of Science & Mathematics
Department
Department of Biochemistry, Chemistry, and Physics
Abstract
Protein tyrosine phosphatase 1B (PTP-1B) is a non-receptor phosphatase that negatively regulates insulin and leptin signaling and has been implicated in oncogenic signaling pathways, including HER2-driven breast cancer and other proliferative disorders. PTP-1B overexpression contributes to tumor progression, metabolic dysfunction, and resistance to targeted therapies, making it an attractive therapeutic target. In this study, we report a green synthetic approach toward a library of 3,4,6-trisubstituted pyridazines and their biological evaluation against PTP-1B.
The pyridazine scaffold, a six-membered aromatic heterocycle containing adjacent nitrogen atoms, was constructed via hydrazine-mediated cyclization in ethanol using a pyridinium based ionic liquid as a dual solvent–catalyst system. This methodology minimizes volatile organic solvent use, reduces hazardous waste, and enhances energy efficiency, aligning with key principles of green chemistry. Reaction progress was monitored by TLC, and products were purified via automated flash chromatography. Structural elucidation was performed through NMR spectroscopy.
A library of trisubstituted pyridazines was synthesized in moderate to good yields and subsequently evaluated in a phosphatase inhibition assay. Biological results demonstrated that none of the synthesized compounds exhibited greater than 50% inhibition of PTP-1B activity relative to vanadate under the tested conditions.
Although significant inhibitory activity was not observed, this work establishes an environmentally benign synthetic platform for pyridazine derivatives and provides structure–activity insights to guide future optimization toward more potent PTP-1B inhibitors.
Program Description
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Start Date
4-23-2026 10:30 AM
End Date
4-23-2026 10:45 AM
Recommended Citation
Osaghae, Joshua O., "Green Synthesis of 3,4,6-Trisubstituted Pyridazines and Their Biological Evaluation Against PTP-1B" (2026). GS4 Student Scholars Symposium. 111.
https://digitalcommons.georgiasouthern.edu/research_symposium/2026/2026/111
Green Synthesis of 3,4,6-Trisubstituted Pyridazines and Their Biological Evaluation Against PTP-1B
Russell Union 2075
Protein tyrosine phosphatase 1B (PTP-1B) is a non-receptor phosphatase that negatively regulates insulin and leptin signaling and has been implicated in oncogenic signaling pathways, including HER2-driven breast cancer and other proliferative disorders. PTP-1B overexpression contributes to tumor progression, metabolic dysfunction, and resistance to targeted therapies, making it an attractive therapeutic target. In this study, we report a green synthetic approach toward a library of 3,4,6-trisubstituted pyridazines and their biological evaluation against PTP-1B.
The pyridazine scaffold, a six-membered aromatic heterocycle containing adjacent nitrogen atoms, was constructed via hydrazine-mediated cyclization in ethanol using a pyridinium based ionic liquid as a dual solvent–catalyst system. This methodology minimizes volatile organic solvent use, reduces hazardous waste, and enhances energy efficiency, aligning with key principles of green chemistry. Reaction progress was monitored by TLC, and products were purified via automated flash chromatography. Structural elucidation was performed through NMR spectroscopy.
A library of trisubstituted pyridazines was synthesized in moderate to good yields and subsequently evaluated in a phosphatase inhibition assay. Biological results demonstrated that none of the synthesized compounds exhibited greater than 50% inhibition of PTP-1B activity relative to vanadate under the tested conditions.
Although significant inhibitory activity was not observed, this work establishes an environmentally benign synthetic platform for pyridazine derivatives and provides structure–activity insights to guide future optimization toward more potent PTP-1B inhibitors.
