disintegrins
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 (ITGs). The term disintegrin was first proposed by R. J. Gould et al. in 1989.
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.
See also
ADAMs (A disintegrin and metalloproteinases)