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In this study, we report the characterization of a disintegrin isolated from <jats:italic>Cerastes cerastes<\/jats:italic> venom, exhibiting antiparasitic activity on <jats:italic>Leishmania infantum<\/jats:italic> promastigotes. Indeed, isolated disintegrin, referred to Disintegrin_Cc, induced 84.75% of parasiticidal activity and deep morphological alterations on the parasites. SDS\u2010PAGE analysis indicated that this disintegrin was homogenous. This dimeric disintegrin of 14,193.97\u00a0Da contains an RGD domain and four intramolecular disulfide bridges. It presents a high percentage of identity with other related snake disintegrins. Predicted 3D structure indicated that this peptide shares partial homology with well\u2010known active antimicrobial peptides. Disintegrin_Cc inhibited 80% of arachidonic acid\u2010induced platelet aggregation. The obtained results suggest that the isolated molecule plays a dual role as a disintegrin and as an anti\u2010leishmanial compound. 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