Abstract
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.
Original language | English |
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Title of host publication | Ion Channels |
Subtitle of host publication | Channel Chemical Biology, Engineering, and Physiological Function |
Editors | Daniel L. Minor, Henry M. Colecraft |
Publisher | Academic Press Inc. |
Pages | 169-201 |
Number of pages | 33 |
ISBN (Print) | 9780128239247 |
DOIs | |
Publication status | Published - Jan 2021 |
Publication series
Series | Methods in Enzymology |
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Volume | 654 |
ISSN | 0076-6879 |
Funding
Publisher Copyright: © 2021 Elsevier Inc.
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Biochemistry