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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 α1β1 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 α2β1, αIIbβ3, αvβ3, α4β1, α5β1, α6β1, and α9β1, α4β7 integrins. Obtustatin potently inhibits angiogenesis in chicken and in mouse model and reduces tumor development by half.

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Peptides & proteins
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Molecular Weight:
4393.13 Da
Daidone I, et al. (2013) Structural and dynamical properties of KTS-disintegrins: A comparison between Obtustatin and Lebestatin. Biopolymers.; Brown MC, et al. (2008) Angiostatic activity of obtustatin as alpha1beta1 integrin inhibitor in experimental melanoma growth. Int J Cancer.; Calvete JJ, et al. (2007) KTS and RTS-disintegrins: anti-angiogenic viper venom peptides specifically targeting the alpha 1 beta 1 integrin. Curr Pharm Des.; Moreno-Murciano M.P., et al. (2003) Amino acid sequence and homology modeling of obtustatin, a novel non-RGD-containing short disintegrin isolated from the venom of Vipera lebetina obtusa. Protein Sci.; Marcinkiewicz C., et al. (2003) Obtustatin: a potent selective inhibitor of alpha1beta1 integrin in vitro and angiogenesis in vivo. Cancer Res.; Moreno-Murciano M.P., et al. (2003) NMR solution structure of the non-RGD disintegrin obtustatin. J. Mol. Biol.