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Snake Venoms pp 437–449Cite as

Snake Venom Disintegrins

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Part of the book series: Toxinology ((TOXI))

Abstract

Disintegrins are generally involved in cell-cell and cell-matrix adhesion. Although disintegrins were first identified in viper venoms, their presence in many other organs, tissues, and secretions was reported later. In snake venoms, these small cysteine-rich peptides strongly inhibit platelet aggregation and thereby antagonize clotting of blood in bite victims. The integrin binding is generally dependent upon a conserved arginine-glycine-aspartic acid (RGD) motif. However, many disintegrins lacking this RGD motif can also bind and block integrins. Disintegrins from hematophagous animals show considerable variation in the signature tripeptide disintegrin motif. However, in most cases the aspartic acid residue (D) is present. Disintegrins found in snake venoms and mammalian ADAM (disintegrin and metalloproteinase) are believed to share a common membrane-bound protein ancestor, which underwent modifications and acquired novel functions through millions of years. Recently, disintegrins have attracted researchers for their ability to strongly intervene in tumor growth and angiogenesis. Some drugs have already been designed in mimicking the molecular structures of disintegrins. Currently, many laboratories are engaged in isolating and characterizing disintegrins with a focus on developing novel anticancer and antithrombotic drugs.

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Chakrabarty, D., Chanda, C. (2017). Snake Venom Disintegrins. In: Inagaki, H., Vogel, CW., Mukherjee, A., Rahmy, T. (eds) Snake Venoms. Toxinology. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-6410-1_14

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