ArticleBiotechnology progress
Active, soluble recombinant melittin purified by extracting insoluble lysate of Escherichia coli without denaturation.
Article in Biotechnology progress. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 11 citations in OpenAlex.
- A Comparative Study of Melittins fromInternational journal of molecular sciences · 2025Article
- Assessment of antibiotic release and antibacterial efficacy from pendant glutathione hydrogels using ex vivo porcine skin.Journal of controlled release : official journal of the Controlled Release Society · 2024Article
- Nuclear Magnetic Resonance-Based Structural Characterization and Backbone Dynamics of Recombinant Bee Venom Melittin.Biochemistry · 2018Article
- Melittin-glutathione S-transferase fusion protein exhibits anti-inflammatory properties and minimal toxicity.European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences · 2014Article
- Proteolytically activated anti-bacterial hydrogel microspheres.Journal of controlled release : official journal of the Controlled Release Society · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Cell lytic peptides are a class of drugs that can be used to selectively kill invading organisms or diseased cells. Several of these peptides have been identified as potential therapeutics. Herein, we report a novel process for purifying recombinant melittin, a cell lytic peptide that inserts into the membranes of cells causing cell lysis, from Escherichia coli. The process involves surfactant and low pH to solubilize melittin fusion proteins from the insoluble fraction of bacterial lysates. We are able to significantly improve purity of the final product and confirm the activity of the peptide. The process yields recombinant melittin that is effective when used to treat U-87 MG glioma cells and inhibits growth of the gram-positive pathogenic bacterium Streptococcus pyogenes. We demonstrate a method of repeated extraction of the insoluble protein fraction with mild detergent at a low pH that is able to generate a yield of pure, soluble melittin of ∼ 0.5-1 mg/L of E. coli culture.
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Registered trials
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