obtustatin

Obtustatin is a highly potent, selective, non-RGD-containing short disintegrin peptide originally isolated from the venom of the viper *Vipera lebetina obtusa*. Composed of 41 amino acids, it is the shortest known disintegrin and features a KTS (Lys-Thr-Ser) active site motif instead of the classical RGD sequence. Obtustatin specifically and potently inhibits the binding of integrin α1β1 (CD49a/CD29) to collagen IV with an IC50 of approximately 0.8 to 2 nM, without affecting other closely related integrins such as α2β1 or αIIbβ3. By blocking integrin α1β1 signaling, obtustatin inhibits endothelial cell proliferation, induces apoptosis, and suppresses angiogenesis. It has demonstrated significant anti-angiogenic and antitumor efficacy in preclinical animal models of melanoma, Lewis lung carcinoma, and sarcoma, and is widely utilized as a research tool to study integrin biology, angiogenesis, and inflammatory processes.

Other names

disintegrin obtustatinKTS-disintegrin