title: In silico molecular interaction analysis of LTNF peptide-LT10 with snake venom enzymes.
abstract: Lethal Toxin Neutralizing Factor (LTNF) isolated from Opossum (Didephis virginiana) has been shown to exhibit anti-venom and anti-allergic property. The small synthetic peptide- LT10 derived from N-terminal of LTNF also showed this property in vivo. We applied molecular modeling, docking and molecular dynamic (MD) simulation techniques to compute the interaction of LT10 peptide with few snake venom enzymes, namely PLA2 from Naja naja and Atrolysin -C from Crotalus atrox. Our in silico interaction analyses provides molecular basis that might account for antivenom activity of LT10 peptide towards these two snake venom toxins. The understanding of such key molecular interactions could be useful for design and development of better anti-snake venom therapies.
authors.forename: Sonali G
authors.initials: SG
authors.lastname: Chavan
authors.affiliation: Bioinformatics Centre & Department of Zoology, Center of Advanced Studies, University of Pune, Pune 411007, India. deepti.deobagkar@gmail.com.
authors.forename: Deepti D
authors.initials: DD
authors.lastname: Deobagkar
mesh_terms: D000818:Animals; D000997:Antivenins / Q000737:chemistry / Q000378:metabolism; D003198:Computer Simulation; D008666:Metalloendopeptidases / Q000737:chemistry / Q000378:metabolism; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D009893:Opossums; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012910:Snake Venoms / Q000737:chemistry / Q000378:metabolism
chemical_list: D000997:Antivenins; D010446:Peptide Fragments; D011994:Recombinant Proteins; D012910:Snake Venoms; D008666:Metalloendopeptidases; C089232:atrolysin C