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Crotalus adamanteus venom toxins comprise a complex mixture of proteins and peptides secreted by the Eastern diamondback rattlesnake, the largest venomous snake in North America [12,16]. These toxins primarily include snake venom metalloproteinases (SVMPs), serine proteases (SVSPs), and phospholipases A2 (PLA2s), which work synergistically to cause severe hemotoxicity, local tissue necrosis, and systemic coagulopathy [1,4,15]. Biologically, these molecules function by degrading the extracellular matrix, interfering with the coagulation cascade, and inducing potent inflammatory and hypotensive responses [3,11]. In clinical medicine, these toxins are the primary therapeutic targets of polyvalent antivenoms such as CroFab, which utilize purified Fab fragments to bind and neutralize the active venom components [1,6]. Beyond their role in envenomation pathology, individual components of the venom are under investigation as potential therapeutic leads for chronic pain, cardiovascular disorders, and antimicrobial applications [9,14]. Effective management of envenomed patients requires continuous monitoring of hematologic biomarkers, such as fibrinogen levels and platelet counts, to detect and treat toxin-induced systemic effects [2,15].
Neutralization of venom toxins through binding by specific antibody fragments (Fab or F(ab')2), which prevents toxin interaction with physiological targets and facilitates their redistribution and elimination from the body [1,2,6].
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