Isolation and characterisation of conomap-Vt, a D-amino acid containing excitatory peptide from the venom of a vermivorous cone snail

被引：37

作者：

Dutertre, Sebastien ^{[1
]}

Lumsden, Natalie G. ^{[1
]}

Alewood, Paul F. ^{[1
]}

Lewis, Richard J. ^{[1
]}

机构：

[1] Univ Queensland, Inst Mol Biosci, Brisbane, Qld 4072, Australia

来源：

FEBS LETTERS | 2006年 / 580卷 / 16期

基金：

英国医学研究理事会; 澳大利亚研究理事会;

关键词：

cone snail; conotoxin; venom peptide; post-translational modification; molusc selective bioactive;

D O I：

10.1016/j.febslet.2006.06.011

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Cone snail venom is a rich source of bioactives, in particular small disulfide rich peptides that disrupt synaptic transmission. Here, we report the discovery of conomap-Vt (Conp-Vt), an unusual linear tetradecapeptide isolated from Conus vitulinus venom. The sequence displays no homology to known conopeptides, but displays significant homology to peptides of the MATP (myoactive tetradecapeptide) family, which are important endogenous neuromodulators in molluscs, annelids and insects. Conp-Vt showed potent excitatory activity in several snail isolated tissue preparations. Similar to ACh, repeated doses of Conp-Vt were tachyphylactic. Since nicotinic and muscarinic antagonists failed to block its effect and Conp-Vt desensitised tissue remained responsive to ACh, it appears that Conp-Vt contractions were non-cholinergic in origin. Finally, biochemical studies revealed that Conp-Vt is the first member of the MATP family with a D-amino acid. Interestingly, the isomerization of L-Phe to D-Phe enhanced biological activity, suggesting that this post-translational modified conopeptide may have evolved for prey capture. (c) 2006 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：3860 / 3866

页数：7

共 24 条

[1] Post-translational amino acid isomerization - A functionally important D-amino acid in an excitatory peptide [J].