ArticlePloS one2016
Rational Design of a Carrier Protein for the Production of Recombinant Toxic Peptides in Escherichia coli.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 49 citations in OpenAlex.
- Accessing intractable, phosphorylated intrinsically disordered proteins via a protease-cleavable inclusion body tag.Protein science : a publication of the Protein Society · 2026Article
- Exploring the Antimicrobial and Antiviral Properties of Cryptic Peptides from Human Fibrinogen.International journal of molecular sciences · 2025Article
- Cathelicidins: Opportunities and Challenges in Skin Therapeutics and Clinical Translation.Antibiotics (Basel, Switzerland) · 2024Review
- Heterologous Production of Antimicrobial Peptides: Notes to Consider.The protein journal · 2024Article
- The Antimicrobial, Antibiofilm and Anti-Inflammatory Activities of P13#1, a Cathelicidin-like Achiral Peptoid.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Refinement of the Fusion Tag PagP for Effective Formation of Inclusion Bodies in Escherichia coli.Microbiology spectrum · 2023Article
- Structure-activity relationships of antibacterial peptides.Microbial biotechnology · 2023Review
- Synthetic biology-inspired cell engineering in diagnosis, treatment, and drug development.Signal transduction and targeted therapy · 2023Review
- Novel Antimicrobial Strategies to Prevent Biofilm Infections in Catheters after Radical Cystectomy: A Pilot Study.Life (Basel, Switzerland) · 2022Article
- Environment-Sensitive Fluorescent Labelling of Peptides by Luciferin Analogues.International journal of molecular sciences · 2021Article
- Impact of a Single Point Mutation on the Antimicrobial and Fibrillogenic Properties of Cryptides from Human Apolipoprotein B.Pharmaceuticals (Basel, Switzerland) · 2021Article
- Review
- Detecting aspartate isomerization and backbone cleavage after aspartate in intact proteins by NMR spectroscopy.Journal of biomolecular NMR · 2021Article
- Chemical Digestion of the -Asp-Cys- Sequence for Preparation of Post-translationally Modified Proteins.The protein journal · 2020Article
- Recombinant expression, purification and PEGylation of Paneth cell peptide (cryptdin-2) with value added attributes against Staphylococcus aureus.Scientific reports · 2020Article
- Novel Self-Assembled Micelles Based on Cholesterol-Modified Antimicrobial Peptide (DP7) for Safe and Effective Systemic Administration in Animal Models of Bacterial Infection.Antimicrobial agents and chemotherapy · 2018Article
- Rapid and efficient production of cecropin A antibacterial peptide in Escherichia coli by fusion with a self-aggregating protein.BMC biotechnology · 2018Article
- Exploring the role of unnatural amino acids in antimicrobial peptides.Scientific reports · 2018Article
- The growing impact of lyophilized cell-free protein expression systems.Bioengineered · 2017Review
- Production of Recombinant Antimicrobial Polymeric Protein Beta Casein-E 50-52 and Its Antimicrobial Synergistic Effects Assessment with Thymol.Molecules (Basel, Switzerland) · 2017Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Commercial uses of bioactive peptides require low cost, effective methods for their production. We developed a new carrier protein for high yield production of recombinant peptides in Escherichia coli very well suited for the production of toxic peptides like antimicrobial peptides. GKY20, a short antimicrobial peptide derived from the C-terminus of human thrombin, was fused to the C-terminus of Onconase, a small ribonuclease (104 amino acids), which efficiently drove the peptide into inclusion bodies with very high expression levels (about 200-250 mg/L). After purification of the fusion protein by immobilized metal ion affinity chromatography, peptide was obtained by chemical cleavage in diluted acetic acid of an acid labile Asp-Pro sequence with more than 95% efficiency. To improve peptide purification, Onconase was mutated to eliminate all acid labile sequences thus reducing the release of unwanted peptides during the acid cleavage. Mutations were chosen to preserve the differential solubility of Onconase as function of pH, which allows its selective precipitation at neutral pH after the cleavage. The improved carrier allowed the production of 15-18 mg of recombinant peptide per liter of culture with 96-98% purity without the need of further chromatographic steps after the acid cleavage. The antimicrobial activity of the recombinant peptide, with an additional proline at the N-terminus, was tested on Gram-negative and Gram-positive strains and was found to be identical to that measured for synthetic GKY20. This finding suggests that N-terminal proline residue does not change the antimicrobial properties of recombinant (P)GKY20. The improved carrier, which does not contain cysteine and methionine residues, Asp-Pro and Asn-Gly sequences, is well suited for the production of peptides using any of the most popular chemical cleavage methods.
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Registered trials
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