Production of recombinant venom peptides as tools for ion channel research

被引:6
|
作者
Saikia, Chandamita [1 ]
Ben-Nissan, Gili [1 ]
Reuveny, Eitan [1 ]
Karbat, Izhar [1 ]
机构
[1] Weizmann Inst Sci, Dept Biomol Sci, Rehovot, Israel
来源
ION CHANNELS: CHANNEL CHEMICAL BIOLOGY, ENGINEERING, AND PHYSIOLOGICAL FUNCTION | 2021年 / 654卷
关键词
INTEIN-MEDIATED EXPRESSION; EPIDERMAL-GROWTH-FACTOR; SODIUM-CHANNELS; FUNCTIONAL EXPRESSION; MINI-INTEIN; PROTEIN; SCORPION; PURIFICATION; TOXIN; RECEPTOR;
D O I
10.1016/bs.mie.2021.01.029
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Animal venom is a rich source for peptide toxins that bind and modulate the function of ion channels. Owing to their ability to bind receptor sites on the channel protein with high affinity and specificity, peptide neurotoxins have become an indispensable tool for ion channel research. Recent breakthroughs in structural biology and advances in computer simulations of biomolecules have sparked a new interest in animal toxins as probes of channel protein structure and function. Here, we focus on methods used to produce animal toxins for research purposes using recombinant expression. The specific challenges associated with heterologous production of venom peptides are discussed, and several methods targeting these issues are presented with an emphasis on E. coli based systems. An efficient protocol for the bacterial expression, folding, and purification of recombinant venom peptides is described.
引用
收藏
页码:169 / 201
页数:33
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