ArticleAMB Express2019
Design and activity study of a melittin-thanatin hybrid peptide.
Article in AMB Express, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
13 citing papers in PubMed, 1 synthesis or guideline pooled it, 21 citations in OpenAlex.
- Therapeutic potential and safety challenges of antimicrobial peptides and peptidomimetics against ESKAPEE pathogens: a systematic review with quantitative analysis.The Journal of antimicrobial chemotherapy · 2026Pooled it
- Multidimensional Modification and Functional Optimization of Melittin: From Natural Toxic Peptide to Safe and Effective Therapeutics.Pharmaceutics · 2026Review
- Concentration-Dependent Anticancer Effects of Melittin-Functionalized Nanomaterials.Materials (Basel, Switzerland) · 2026Review
- Hybrid and conjugated antimicrobial peptides: new tactics to counter bacterial resistance.Frontiers in microbiology · 2026Review
- Therapeutic Bioactivity Exerted by theMolecules (Basel, Switzerland) · 2025Article
- Thanatin: A Promising Antimicrobial Peptide Targeting the Achilles' Heel of Multidrug-Resistant Bacteria.International journal of molecular sciences · 2024Review
- Molecular hybridization strategy for tuning bioactive peptide function.Communications biology · 2023Article
- Yeast Expressed Hybrid Peptide CLP Abridged Pro-Inflammatory Cytokine Levels by Endotoxin Neutralization.Microorganisms · 2023Article
- Peptide Conjugates Derived from flg15, Pep13, and PIP1 That Are Active against Plant-Pathogenic Bacteria and Trigger Plant Defense Responses.Applied and environmental microbiology · 2022Article
- Melittin-Based Nano-Delivery Systems for Cancer Therapy.Biomolecules · 2022Review
- Rational Design of a Hybrid Peptide against Severe Acute Respiratory Syndrome Coronavirus 2 Using Melittin and Angiotensin-Converting Enzyme 2 as Pharmaceutical Agents.Advanced biomedical research · 2022Article
- Thanatin: An Emerging Host Defense Antimicrobial Peptide with Multiple Modes of Action.International journal of molecular sciences · 2021Review
- Expression of Melittin in Fusion with GST inACS omega · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
The unique antimicrobial mechanism of antimicrobials make them a promising substitute for antibiotics for fighting drug-resistant bacteria. Both melittin and thanatin have antimicrobial bioactivity. However, thanatin does not inhibit the growth of Staphylococcus aureus. Melittin can inhibit S. aureus and has strong hemolytic activity. In the present study, the mutant fragments of melittin and thanatin were combined by flexible peptides to form a novel hybrid peptide, which was synthesized based on the secondary and tertiary structure prediction. The hybrid peptide inhibited S. aureus with a hemolytic concentration of above 45 μmol/L and inhibition rate in SMMC-7721 cells of 19.14%. The hybrid antimicrobial peptide, which was designed by the combination of α-helix and β-lamellar antimicrobial peptides, showed that both types of peptides did not interact with each either on spatial structure or biological activities, thereby providing a novel idea for the design of artificial antimicrobial peptides.
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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.