Disintegrins are peptides isolated from the venom of various snakes of the viper family. Peptides (from the Greek πεπτίδια, "small digestibles" are short Polymers formed from the linking in a defined order of α- Amino They interact with the beta 1 and beta 3 families of integrin proteins. Integrins are Cell surface receptors that interact with the Extracellular matrix (ECM and mediate various intracellular signals. 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. Not to be confused with Cystine, its oxidized dimer Cysteine (abbreviated as Cys or C) is an α- Amino acid with
They work by countering the blood clotting steps, inhibiting the clumping of platelets. Platelets, or Thrombocytes, are small cytoplasmic bodies derived from cells They circulate in the Blood of Mammals and are involved
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.