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Background
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Obtustatin is a 41 amino acid disintegrin peptide isolated from the venom of the Vipera lebetina obtusa. It is a potent (IC50 = 2 nM) and selective inhibitor of the binding of alpha1beta1 integrin to collagen IV. Contrary to other known disintegrins, it does not contain the classical RGD sequence. Does not show inhibitory activity toward other integrins, including alpha2beta1, alphaIIbbeta3, alphavbeta3, alpha4beta1, alpha5beta1, alpha6beta1, and alpha9beta1, alpha4beta7 integrins. Obtustatin potently inhibits angiogenesis in chicken and in mouse model and reduces tumor development by half.
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