ω-阿加毒素IVA及其相关肽的合成。
Synthesis of omega-agatoxin IVA and its related peptides.
作者信息
Nishio H, Kumagaye K Y, Kubo S, Chen Y N, Momiyama A, Takahashi T, Kimura T, Sakakibara S
机构信息
Peptide Institute, Inc., Protein Research Foundation, Osaka, Japan.
出版信息
Biochem Biophys Res Commun. 1993 Nov 15;196(3):1447-53. doi: 10.1006/bbrc.1993.2414.
A potent and selective P type calcium channel blocker isolated from the venom of the funnel web spider Agelenopsis aperta, omega-agatoxin IVA, and its related peptides were synthesized by the solution procedure. Synthetic omega-agatoxin IVA was found to block high-threshold P-type calcium current in rat Purkinje neuron with the same potency as that reported for the natural product. Its disulfide structure was determined by amino acid analysis, gas-phase sequencing and mass spectrometry of the proteolytic fragments. The N-terminus biotinylated and truncated peptides showed the same disulfide-bond-forming profile and the same activities as those of omega-agatoxin IVA, indicating that the N-terminal basic tripeptide, Lys-Lys-Lys, is not important for both the folding and the expression of the biological activity. However, the Trp residue in the molecule might be essential for the toxin to bind tightly with the channel pores.
从漏斗网蜘蛛（Agelenopsis aperta）毒液中分离出的一种强效且具选择性的P型钙通道阻滞剂ω-芋螺毒素IVA及其相关肽段，通过溶液法合成。发现合成的ω-芋螺毒素IVA能以与天然产物报道的相同效力阻断大鼠浦肯野神经元中的高阈值P型钙电流。其二硫键结构通过氨基酸分析、气相测序以及蛋白水解片段的质谱分析得以确定。N端生物素化和截短的肽段显示出与ω-芋螺毒素IVA相同的二硫键形成模式和相同活性，表明N端碱性三肽Lys-Lys-Lys对折叠和生物活性表达均不重要。然而，分子中的色氨酸残基可能是毒素与通道孔紧密结合所必需的。
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