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大电导钙激活钾离子(BK)通道广泛分布于可兴奋细胞与非兴奋细胞中,行使着一系列重要的生理功能。以源于蝎粗毒的高亲和性毒素作为研究工具,使BK通道的药理学和结构性质正逐步被揭示。Martentoxin是一种分离提取自东亚短钳蝎(Buthus martensi Karsch)粗毒的短链多肽,由37个氨基酸残基构成。研究表明,其对BK通道的特异性远高于其它各类型的电压门控钾通道(Kv)。迄今为止,由于用以探明BK通道亚型结构与功能及相关病理的特异性药物工具仍然稀缺,因此阐明martentoxin与BK通道间的相互作用模式就显得至关重要了。鉴于此原因,本综述将针对martentoxin的药理性质和其与BK通道相互作用的分子机制做进一步阐明。
Large conductance calcium-activated potassium (BK) channels are widely distributed in excitable cells and non-excited cells, exercise a series of important physiological functions. Taking the high-affinity toxin derived from scorpion venom as a research tool, the pharmacological and structural properties of BK channels are gradually revealed. Martentoxin is a short chain polypeptide isolated from the crude toxin of Buthus martensi Karsch and consists of 37 amino acid residues. Studies have shown that its specificity for the BK channel is much higher than the other types of voltage-gated potassium channels (Kv). To date, elucidation of the mode of interaction between martentoxin and BK channels has become crucial due to the scarcity of specific drug tools to elucidate the subtype and function of BK channels and their associated pathologies. For this reason, this review will further elucidate the pharmacological properties of martentoxin and its molecular mechanisms of interaction with BK channels.