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Snake venom components encompass a vast array of chemically and functionally distinct molecules, primarily proteins and peptides, secreted by specialized glands in venomous snakes[1][3][2]. These molecules modulate critical biological processes such as coagulation, neurotransmission, and cell integrity, and are responsible for both the deadly effects and promising therapeutic applications of venom. The main classes include enzymes (serine proteases, metalloproteinases, phospholipases), toxins (neurotoxins, cytotoxins, cardiotoxins), disintegrins, and other low molecular weight peptides, each with specialized targets in animal physiology[1][2][3][6]. Some components have been exploited for drug development (e.g., ACE inhibitors, integrin antagonists), while antivenoms serve as lifesaving interventions for envenomation. The extreme diversity and synergistic actions of these molecules pose major challenges for therapeutic development and clinical safety[1][2][3][6].
Enzymatic hydrolysis (proteolytic cleavage of blood proteins, phospholipids, etc.)\nIrreversible binding/blockade of receptors (e.g., neurotoxins bind acetylcholine receptors at the neuromuscular junction)\nDisruption of cell membranes (phospholipases, cytotoxins)\nModulation of signaling pathways (interference with integrins, kinins, complement)
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