Snake venom metalloproteinase (SVMP), Serine protease, Disintegrin, Phospholipase A2, C-type lectin protein (Viperidae venom protein family) (SVMP, PLA2, etc. (individual proteins have abbreviations; none specific for "Viperidae venom proteins" as a whole))

Viperidae venom proteins comprise a large, diverse set of bioactive proteins and peptides produced by snakes in the viper family. They play key roles in prey immobilization and digestion by disrupting hemostasis (blood clotting), degrading tissues, and causing cell death. Major families include snake venom metalloproteinases (SVMPs), serine proteases, disintegrins, phospholipases A2 (PLA2s), and C-type lectins. SVMPs are further classified into types P-I, P-II, and P-III based on their domain architecture, with functions ranging from hemorrhage induction, platelet aggregation inhibition, and tissue damage[1][3][5]. Disintegrins specifically inhibit platelet aggregation and cell adhesion, potentially serving as templates for anti-thrombotic drugs[5]. PLA2s exhibit hemolytic and inflammatory activity, but also show anticancer and antimicrobial properties[4][5]. Viperidae venom diversity is high, with proteomic analyses revealing over 100 individual protein forms per species[2][3]. Although these proteins are not targets in classic pharmacology (e.g., receptors or enzymes in human tissue), individual components are direct targets of antivenom drugs and potential sources of new therapeutic compounds for cancer, infection, thrombosis, and pain[4][5]. Safety remains a concern due to their foundational role as toxins[4][5]. For more structured target data, it is recommended to specify a **single protein or molecular entity under the Viperidae venom protein family** (e.g., "Snake venom metalloproteinase from Daboia russelii" or "Disintegrin from Echis carinatus") rather than the broad group as listed.

Other names

Viper venom proteinsViperidae toxinsSVMPsserine proteasesdisintegrinssnake venom enzymesvenom glycoproteins

Proteolytic cleavage of plasma proteins (SVMPs, serine proteases); Inactivation of key components of blood clotting (Factor X activators); Inhibition of platelet aggregation (disintegrins); Membrane degradation/cytotoxicity (PLA2); Modulation of immune/inflammatory responses