Disintegrins are peptides isolated from the venom of various snakes of the viper family. They interact with the beta 1 and beta 3 families of integrin proteins. Disintegrins are cysteine-rich peptides ranging from 45 to 84 amino acids in length and almost all of them contain an Arg-Gly-Asp (RGD) sequence, a recognition site of many adhesion proteins.

They work by countering the blood clotting steps, inhibiting the clumping of platelets.

Examples of disintegrins are: albolabrin, applagin, barbourin, batroxostatin, bitistatin, echistatin, elegantin, eristicophin, flavoridin, halysin, kistrin, tergeminin and triflavin.

The term disintegrin was first proposed by R. J. Gould et al. in 1989.

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