ArticlePloS one2013
Production of recombinant disulfide-rich venom peptides for structural and functional analysis via expression in the periplasm of E. coli.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.
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Who cites it
87 citing papers in PubMed, 158 citations in OpenAlex.
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- Scorpion Venom as a Source of Cancer Drugs: A Comprehensive Proteomic Analysis and Therapeutic Potential.International journal of molecular sciences · 2025Review
- Recombinant α-Toxin BmK-M9 Inhibits Breast Cancer Progression by Regulating β-Catenin In Vivo.Cell biochemistry and biophysics · 2025Article
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- An improved variant of tobacco etch virus (TEV) protease that does not need reducing agents.Protein science : a publication of the Protein Society · 2025Article
- Gene expression, purification, and functional characterization of recombinant conotoxin μ-TIIIA and TIIIAlaMut inBiotechnologia · 2025Article
- Prospects and challenges of recombinant spider venom enzymes: insights fromFrontiers in bioengineering and biotechnology · 2025Article
- Enlightening the toxinological dark matter of spider venom enzymes.npj biodiversity · 2024Article
- Bioproduction Platform to Generate Functionalized Disulfide-Constrained Peptide Analogues.ACS bio & med chem Au · 2024Article
- Structural Basis of the Bivalency of the TRPV1 Agonist DkTx.Angewandte Chemie (International ed. in English) · 2024Article
- A phage-displayed disulfide constrained peptide discovery platform yields novel human plasma protein binders.PloS one · 2024Article
- A previously unrecognized superfamily of macro-conotoxins includes an inhibitor of the sensory neuron calcium channel Cav2.3.PLoS biology · 2023Article
- Development and Validation of Nerve-Targeted Bacteriochlorin Sensors.Journal of the American Chemical Society · 2023Article
- A bivalent remipede toxin promotes calcium release via ryanodine receptor activation.Nature communications · 2023Article
- Structure-function and rational design of a spider toxin Ssp1a at human voltage-gated sodium channel subtypes.Frontiers in pharmacology · 2023Article
27 more citing papers are in PubMed but not listed here.
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Disulfide-rich peptides are the dominant component of most animal venoms. These peptides have received much attention as leads for the development of novel therapeutic agents and bioinsecticides because they target a wide range of neuronal receptors and ion channels with a high degree of potency and selectivity. In addition, their rigid disulfide framework makes them particularly well suited for addressing the crucial issue of in vivo stability. Structural and functional characterization of these peptides necessitates the development of a robust, reliable expression system that maintains their native disulfide framework. The bacterium Escherichia coli has long been used for economical production of recombinant proteins. However, the expression of functional disulfide-rich proteins in the reducing environment of the E. coli cytoplasm presents a significant challenge. Thus, we present here an optimised protocol for the expression of disulfide-rich venom peptides in the periplasm of E. coli, which is where the endogenous machinery for production of disulfide-bonds is located. The parameters that have been investigated include choice of media, induction conditions, lysis methods, methods of fusion protein and peptide purification, and sample preparation for NMR studies. After each section a recommendation is made for conditions to use. We demonstrate the use of this method for the production of venom peptides ranging in size from 2 to 8 kDa and containing 2-6 disulfide bonds.
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