独居黄蜂毒液中新型肽神经毒素——蛛蜂毒素的分离与结构

Isolation and structure of pompilidotoxins, novel peptide neurotoxins in solitary wasp venoms.

作者信息

Konno K, Hisada M, Itagaki Y, Naoki H, Kawai N, Miwa A, Yasuhara T, Takayama H

机构信息

Faculty of Pharmaceutical Sciences, Teikyo University, Sagamiko, Kanagawa, 199-0195, Japan.

出版信息

Biochem Biophys Res Commun. 1998 Sep 29;250(3):612-6. doi: 10.1006/bbrc.1998.9299.

DOI:10.1006/bbrc.1998.9299

PMID:9784394

Abstract

Novel peptide neurotoxins, alpha- and beta-pompilidotoxins (alpha- and beta-PMTXs), were purified from the venoms of the solitary wasps Anoplius samariensis and Batozonellus maculifrons. Their structures were analyzed mostly by MALDI-TOF-MS, which were corroborated by solid-phase synthesis. alpha-PMTX, with 13 amino acid residues and the sequence of Arg-Ile-Lys-Ile-Gly-Leu-Phe-Gln-Asp-Leu-Ser-Lys-Leu-NH2, greatly potentiates synaptic transmission of lobster leg muscle by the presynaptic mechanisms. beta-PMTX, in which the lysine residue at 12 position of alpha-PMTX was replaced with arginine, was more potent than alpha-PMTX.

摘要

新型肽神经毒素，α-和β-蛛蜂毒素（α-和β-PMTXs），是从独居黄蜂萨摩亚阿诺普利斯和黄斑巴托泽内卢斯的毒液中纯化出来的。它们的结构主要通过基质辅助激光解吸电离飞行时间质谱（MALDI-TOF-MS）进行分析，并通过固相合成得到证实。α-PMTX含有13个氨基酸残基，序列为Arg-Ile-Lys-Ile-Gly-Leu-Phe-Gln-Asp-Leu-Ser-Lys-Leu-NH2，通过突触前机制极大地增强了龙虾腿部肌肉的突触传递。β-PMTX是将α-PMTX第12位的赖氨酸残基替换为精氨酸，其效力比α-PMTX更强。