Functional and structural study comparing the C-terminal amidated β-neurotoxin Ts1 with its isoform Ts1-G isolated from Tityus serrulatus venom

被引：29

作者：

Coelho, V. A. ^{[1
]}

Cremonez, C. M. ^{[1
]}

Anjolette, F. A. P. ^{[1
]}

Aguiar, J. F. ^{[2
]}

Varanda, W. A. ^{[2
]}

Arantes, E. C. ^{[1
]}

机构：

[1] Univ Sao Paulo, Sch Pharmaceut Sci Ribeirao Preto, Dept Chem & Phys, BR-14040903 Ribeirao Preto, SP, Brazil

[2] Univ Sao Paulo, Ribeirao Preto Med Sch, Dept Physiol, BR-14049900 Ribeirao Preto, SP, Brazil

来源：

TOXICON | 2014年 / 83卷

基金：

巴西圣保罗研究基金会;

关键词：

Ts1; isoform; beta-Neurotoxin; Tityus serrulatus venom; C-terminal amidation; Voltage gated sodium channels; ALPHA-SCORPION TOXIN; MOLECULAR-CLONING; CHANNEL TOXINS; ION-CHANNELS; EXPRESSION; PURIFICATION; ACTIVATION; PEPTIDES; CSSII; GAMMA;

D O I：

10.1016/j.toxicon.2014.02.010

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

Mature Ts1, the main neurotoxin from Tityus serrulatus venom, has its C-terminal Cys amidated, while the isolated isoform of Ts1, named Ts1-G, keeps the non-arnidated Gly residue at the C-terminal region, allowing the study of the comparative functional importance of amidation at the C-terminal between these two native toxins. Voltage dependent sodium current measurements showed that the affinity of Ts1-G for sodium channels is smaller than that of the mature Ts1, confirming the important role played by the C-terminal amidation in determining Ts1 activity. (C) 2014 Elsevier Ltd. All rights reserved.

引用

页码：15 / 21

页数：7

共 34 条

[1] A SIMPLIFIED PROCEDURE FOR THE FRACTIONATION OF TITYUS-SERRULATUS VENOM - ISOLATION AND PARTIAL CHARACTERIZATION OF TSTX-IV, A NEW NEUROTOXIN [J].