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Three-finger toxins (3FTxs) are a diverse family of non-enzymatic proteins that constitute a major toxic component of elapid snake venoms, including those from cobras, mambas, and sea snakes [1][2]. Structurally, they are defined by a conserved scaffold of three beta-stranded loops extending from a central core, resembling three fingers, and are stabilized by multiple disulfide bonds [2]. These toxins exhibit a wide range of pharmacological activities, most notably acting as potent antagonists of nicotinic acetylcholine receptors (nAChRs) at the neuromuscular junction, which leads to systemic paralysis and potentially fatal respiratory failure [2][4]. Beyond neurotoxicity, certain 3FTxs function as cardiotoxins or cytotoxins, disrupting cell membranes or modulating ion channels and blood coagulation factors [1][2]. In clinical practice, 3FTxs are the primary targets for antivenom therapies, which utilize purified antibodies to neutralize the toxins biological activity [4]. Recent advancements in drug discovery have also identified 3FTxs as promising templates for designing highly specific therapeutics for pain and cardiovascular conditions, while synthetic broadly neutralizing antibodies like 95Mat5 are being developed to provide more effective treatments for snakebite envenomation [3].
Neutralization of toxin activity through high-affinity binding by antibodies or antivenom fragments, preventing interaction with physiological targets like nicotinic acetylcholine receptors [3][4].
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