Matrix Science Pharma (MSP)

ABSTRACT

Objective: This study aimed to identify potential inhibitors from the beach morning glory (Ipomoea pes-caprae), a plant traditionally used for treating jellyfish stings, to counteract the effects of the venom. Materials and Methods: We utilized homology modeling to construct three-dimensional models of the jellyfish venom metalloproteinase and validated them using the structure analysis and verification server web-based tool for stereochemical quality assessment. Molecular docking studies were conducted using AutoDock Vina to screen compounds extracted from Ipomoea pes-caprae, focusing on their binding affinities toward the venom metalloproteinase. Key compounds, including quercetin and isochlorogenic acids A and B, were analyzed for their potential inhibitory effects. Results: The homology models of the jellyfish venom metalloproteinase were successfully constructed and validated, indicating reliable structural accuracy. The molecular docking studies identified several promising compounds from Ipomoea pes-caprae. Quercetin exhibited a binding energy of −8.8 kcal/mol, whereas isochlorogenic acids A and B showed binding energies of −8.5 and −9.0 kcal/mol, respectively. These compounds demonstrated strong interactions with key amino acids within the active site of the metalloproteinase, suggesting their efficacy in neutralizing the venom’s toxic effects. Conclusion: Our findings support the potential of compounds from Ipomoea pes-caprae as effective inhibitors of jellyfish venom metalloproteinase. This research validates the traditional use of this plant and lays the groundwork for further pharmacological and clinical studies. Future research should focus on in vitro and in vivo testing to confirm the efficacy of these compounds as new therapeutic agents for treating jellyfish stings