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Antiviral Array Library

Library Code: T-VDAviral
 
With viruses such as HIV, HPV, influenza and Ebola representing serious threats to human health globally, there is a significant need for new therapeutics to target them and venoms are proving a rich source of new molecules. The Antiviral Targeted Venom Discovery Array™ is specifically designed to maximize discovery of new tools. Novel antiviral peptides and proteins have been found in snake and scorpion venoms. The Antiviral Targeted Venom Discovery Array libraries contain pure venom fractions from 12, 24, 48 or 96 species optimized for identification of novel antivirals. Each array contains literature-cited, characterized venoms active against viral mechanisms and infection as positive controls. The other venom fractions making up the library have been specially selected by our drug discovery scientists to maximize the novel hit potential.
 
T-VDAviral control venoms include:
  • Trimeresurus stejnegeri (bamboo viper) venom, which contains unique L-amino acid oxidase enzymes that have shown to be antiviral1
  • Contortrostatin, a disintegrin from Agkistrodon contortrix contortrix (southern copperhead) venom is providing a novel approach to blocking HSV (Herpes Simplex Virus) entry2
  • The venoms from a number of scorpion species, particularly those from the Heterometrus  genus, contain antiviral peptides3
References
  1. Zhang YJ, Wang JH, Lee WH, Wang Q, Liu H, Zheng YT, Zhang Y. (2003). Molecular characterization of Trimeresurus stejnegeri venom L-amino acid oxidase with potential anti-HIV activity. Biochem. Biophys. Res. Commun. 26;309(3):598-604
  2. Hubbard S, Choudhary S, Maus E, Shukla D, Swenson S, Markland FS Jr, Tiwari V. (2012). Contortrostatin, a homodimeric disintegrin isolated from snake venom inhibits herpes simplex virus entry and cell fusion. Antivir Ther. 7(7):1319-26
  3. Yan R, Zhao Z, He Y, Wu L, Cai D, Hong W, Wu Y, Cao Z, Zheng C, Li W. (2011). A new natural α-helical peptide from the venom of the scorpion Heterometrus petersii kills HCV. Peptides. 32(1):11-9
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