Escoubas P, Diochot S, Corzo G
Université Pierre-et-Marie-Curie, 9, quai Saint-Bernard, 75252 cedex 05, Paris, France.
Biochimie. 2000 Sep-Oct;82(9-10):893-907. doi: 10.1016/s0300-9084(00)01166-4.
Spider venoms are complex mixtures of neurotoxic peptides, proteins and low molecular mass organic molecules. Their neurotoxic activity is due to the interaction of the venom components with cellular receptors, in particular ion channels. Spider venoms have proven to be a rich source of highly specific peptide ligands for selected subtypes of potassium, sodium and calcium channels, and these toxins have been used to elucidate the structure and physiological roles of the channels in excitable and non-excitable cells. Spider peptides show great variability in their pharmacological activity and primary structure but relative homogeneity in their secondary structure. Following diverse molecular evolution mechanisms, and in particular selective hypermutation, short spider peptides appear to have functionally diversified while retaining a conserved molecular scaffold. This paper reviews the composition and pharmacology of spider venoms with emphasis on polypeptide toxin structure, mode of action and molecular evolution.
蜘蛛毒液是神经毒性肽、蛋白质和低分子量有机分子的复杂混合物。它们的神经毒性活性归因于毒液成分与细胞受体，特别是离子通道的相互作用。事实证明，蜘蛛毒液是钾、钠和钙通道特定亚型的高度特异性肽配体的丰富来源，这些毒素已被用于阐明通道在可兴奋和不可兴奋细胞中的结构和生理作用。蜘蛛肽在药理活性和一级结构上表现出很大的变异性，但在二级结构上相对均匀。遵循多种分子进化机制，特别是选择性超突变，短蜘蛛肽似乎在功能上多样化，同时保留了保守的分子支架。本文综述了蜘蛛毒液的组成和药理学，重点是多肽毒素的结构、作用方式和分子进化。
