ArticleEuropean journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences2014
Melittin-glutathione S-transferase fusion protein exhibits anti-inflammatory properties and minimal toxicity.
Article in European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- A Novel Chitin-Based Purification System Using GAL1 Fusion Tags: Enhancing Recombinant Protein Production While Retaining Biological Activity.Microbial biotechnology · 2025Article
- Article
- Melittin as a therapeutic agent for rheumatoid arthritis: mechanistic insights, advanced delivery systems, and future perspectives.Frontiers in immunology · 2024Review
- 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
- Hosts and Heterologous Expression Strategies of Recombinant Toxins for Therapeutic Purposes.Toxins · 2023Review
- Melittin: a possible regulator of cancer proliferation in preclinical cell culture and animal models.Journal of cancer research and clinical oncology · 2023Review
- Glutathione-Conjugated Hydrogels: Flexible Vehicles for Personalized Treatment of Bacterial Infections.Pharmaceutical research · 2021Article
- Anti-inflammatory activities of arthropod peptides: a systematic review.The journal of venomous animals and toxins including tropical diseases · 2021Review
- Article
- Expression of Melittin in Fusion with GST inACS omega · 2020Article
- Beneficial effects of melittin on ovalbumin-induced atopic dermatitis in mouse.Scientific reports · 2017Article
- Anti-Inflammatory Applications of Melittin, a Major Component of Bee Venom: Detailed Mechanism of Action and Adverse Effects.Molecules (Basel, Switzerland) · 2016Review
- Functional characterization of a melittin analog containing a non-natural tryptophan analog.Biopolymers · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Although potent, proteins often require chemical modification for therapeutic use. Immunogenicity, difficult synthesis, and scale-up of these modifications are all engineering obstacles that stand in the way of expanding the use of these therapeutics. Melittin, a peptide derived from bee venom, has been shown to modulate inflammation. Although potentially therapeutic, the native peptide causes cell lysis and toxicity significantly hindering therapeutic application. Based upon the knowledge of the pore formation mechanism, we examined the toxicity and therapeutic effect of a melittin fusion protein with glutathione-S-transferase. The fusion of melittin and glutathione S-transferase results in diminished toxicity of the peptide and retained anti-inflammatory properties at doses that exceed toxic concentration of native melittin. Our results suggest that fusion proteins, particularly those of glutathione-S-transferase, may be facile modifications to control protein activity.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.