Purification and pharmacological characterization of BmKK2 (α-KTx 14.2), a novel potassium channel-blocking peptide, from the venom of Asian scorpion Buthus martensi Karsch

被引：7

作者：

Li, MH

Zhang, NX

Chen, XQ

Wu, G

Wu, HM

Hu, GY

机构：

[1] Chinese Acad Sci, Shanghai Inst Organ Chem, State Key Lab Bioorgan & Nat Prod Chem, Shanghai 200032, Peoples R China

[2] Chinese Acad Sci, Shanghai Inst Biol Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai 201203, Peoples R China

来源：

TOXICON | 2004年 / 43卷 / 08期

关键词：

BmKK2; Buthus martensi Karsch; delayed rectifier K+ current; hippocampus; neurotoxin; scorpion;

D O I：

10.1016/j.toxicon.2003.11.028

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

BmKK2 (alpha-KTx 14.2) is one of the novel short-chain peptides found in molecular cloning of a venom gland cDNA library from Asian scorpion Buthus martensi Karsch. Based upon its amino acid sequence, the peptide was proposed to adopt a classical alpha/beta-scaffold for alpha-KTxs. In the present study, we purified BmKK2 from the venom of B. martensi Karsch, and investigated its action on voltage-dependent K+ currents in dissociated hippocampal neurons from neonatal rats. BmKK2 (10-100 muM) selectively inhibited the delayed rectifier K+ current, but did not affect the fast transient K+ current. The inhibition of BmKK2 on the delayed rectifier K+ current was reversible and voltage-independent. The peptide did not affect the steady-state activation of the current, but caused a depolarizing shift (about 9 mV) of its steady-state inactivation curve. The results demonstrate that BmKK2 is a novel K+ channel-blocking scorpion peptide. (C) 2004 Elsevier Ltd. All rights reserved.

引用

页码：895 / 900

页数：6

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