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ajgreenchem.com

The objective of this study is to isolate and characterize ursolic acid (UA), a phytochemical compound from Sida mysorensis and to evaluate its anti-inflammatory and neuroprotective potential. To yield a pure compound from the whole plant of Sida mysorensis, gradient silica gel column chromatography was used. The structural identity of ursolic acid was verified through FTIR, ¹H-NMR, ¹³C-NMR, and mass spectrometric analyses. Molecular docking studies with Alzheimer’s disease–associated targets were performed using AutoDock Vina. Ursolic acid exhibited high binding affinities toward all three proteins implicated in neuroinflammation and Alzheimer disease progression. Docking analysis revealed stable hydrogen bonds and hydrophobic interactions within the active sites of GSK3β, ACE, and TACE. The most significant binding affinity was identified with TACE, highlighting the potential of ursolic acid in modulating the release of inflammatory cytokines. The pronounced binding affinity of ursolic acid, especially for TACE and GSK3β, highlights its potential role in regulating neuroinflammation, the amyloid β, and tau hyperphosphorylation, which are key pathological features of Alzheimer's disease. These findings emphasize ursolic acid’s promise in neurodegenerative drug development and reinforce the value of molecular docking as a predictive approach for identifying neuroprotective compounds. Ursolic acid isolated from Sida mysorensis showed strong binding affinities toward TACE, GSK3β, and ACE, with the highest affinity for TACE, suggesting potential regulation of neuroinflammation and AD pathology. These results highlight UA’s promise as a neuroprotective lead compound and support molecular docking as an effective tool for therapeutic prediction.