**5. Examples of Virtual Screening / Molecular Docking in Animal Venom**

[38] performed a virtual screening against α-Cobratoxin. The neurotoxin α-Cobratoxin (Cbtx), isolated from the venom of the Thai cobra *Naja kaouthia*, causes paralysis by prevent‐ ing acetylcholine (ACh) binding to nicotinic acetylcholine receptors (nAChRs). A search for α- Cobratoxin structures was carried out in the PDB, and the virtual screening of 1990 com‐ pounds was performed using the program AutoDock. On [3 H]epibatidine and on [125I] αbungarotoxin, NSC121865 (compound 23) was most potent in binding with Ac (K*d* = 16.26 nM; K*d* = 36.63 nM). The results showed that, in clinical applications, NSC121865 would be a very useful potential lead in the development of a new treatment for snakebite victims. This inhibitor can be used for the development of a more potent and specific anti-cobratoxin.

[14] investigated the effects of protease inhibitors, including phenylmethylsulfonyl fluoride (PMSF), benzamidine (BMD), and their derivatives on the activity of recombinant gloshedo‐ bin, a snake venom thrombin-like enzyme (SVTLE), from the snake *Gloydius shedaoensis*. The structural model of gloshedobin was built by homology modelling using modelling package MODELLER. The stereochemical quality of the homology model was assessed using the PROCHECK program and the software AutoDock was used to dock inhibitors onto the structural model of gloshedobin. The docking results indicated that the strongest inhibitor, PMSF, bound covalently to the catalytic Ser195.

[36] evaluated the inhibitory effect of 1-(3-dimethylaminopropyl)-1-(4-fluorophenyl)-3 oxo-1,3-dihydroisobenzofuran-5-carbonitrile (DFD) on viper venom-induced haemorrhagic and PLA2 activities. Molecular docking studies of DFD and snake venom metalloproteases (SVMPs) were performed to understand the mechanism of inhibition by DFD, since SVMPs constitute one of the protein groups responsible for venom-induced haemorrhage. The docking results showed that DFD binds to a hydrophobic pocket in SVMPs with the K*i* of 19.26 x 10 -9 (kcal/mol) without chelating Zn2+ in the active site.
