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.
Keywords: Atrolysin C, LT10, LTNF, PLA2, snake envenomation, toxin neutralization.
Protein & Peptide Letters
Title:In silico Molecular Interaction Analysis of LTNF Peptide-LT10 with Snake Venom Enzymes
Volume: 21 Issue: 7
Author(s): Sonali G. Chavan and Deepti D. Deobagkar
Affiliation:
Keywords: Atrolysin C, LT10, LTNF, PLA2, snake envenomation, toxin neutralization.
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.
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Cite this article as:
Chavan G. Sonali and Deobagkar D. Deepti, In silico Molecular Interaction Analysis of LTNF Peptide-LT10 with Snake Venom Enzymes, Protein & Peptide Letters 2014; 21 (7) . https://dx.doi.org/10.2174/0929866521666140320112142
DOI https://dx.doi.org/10.2174/0929866521666140320112142 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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Plants are still the major repository of biologically active substances. In the last two decades, however, natural peptides and proteins of plant origin have gained increasing attention due to their pharmacological activities over a variety of human illnesses, including those mediated by infections and parasitosis and those involving different cellular ...read more
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