in silico Study Reveals Potential Docking Sites of δ 2-isoxazolines derivates for Inhibiting Russell’s Viper PLA2 Toxin

Farmers and labors were commonly deal with Russell’s viper envenomation accident. Russell’s viper bite can be reached 70 per 100.000 people every year, of which the fatality can reach up to 2.4. Snake venom phospholipase A 2 s (svPLA 2 s) has considered as the predominant component and major cause of Russell’s viper envenomation. As svPLA 2 s inhibitor, δ2-isoxazolines derivate already proved efficient inhibited PLA2 (IC 50 ), but their mechanism of action remains unveiled, so we aim to predict the putative binding mode of δ2-isoxazolines. The three-dimensional (3D) structures of the basic svPLA2s VRV-PL-VIIIa (P59071) and the inhibitors retrieved from the PDB. Canonical SMILES of small molecule inhibitors including seven δ2-isoxazoline derivatives collected from PubChem. All small molecules mined and saved as a single SDF file using ChemMine. Molecular docking between D. russelli PLA 2 and δ2-isoxazolines derivate performed using PyRx version 0.9.8. The putative interaction was visualized using PyMol, PoseView, and LigPlot. The 2D complex diagram revealed that the svPLA 2 inhibitors directly interact on the active site. There was no correlation between predicted binding affinities with known IC 50 according to simple linear regression analysis. This moiety leads to discovering other group II svPLA 2 s inhibitors as an alternative to conventional serum anti-venom therapy.