ReviewMolecules (Basel, Switzerland)2019
How Melittin Inserts into Cell Membrane: Conformational Changes, Inter-Peptide Cooperation, and Disturbance on the Membrane.
Review in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 112 citations in OpenAlex.
- Bat-derived antimicrobial peptide MC-CATH3 Confers protection against bacterial infections via a potential ferroptosis-like death process.The Journal of biological chemistry · 2026Article
- Antimicrobial peptides in anti-infective and immunomodulatory applications: Mechanisms, challenges, and emerging computational design.Zoological research · 2026Review
- Bacterial cell fate under stress: lipid remodeling and antimicrobial peptide attack.npj antimicrobials and resistance · 2026Article
- Redox-Responsive Polymeric Nanocapsules for Enhanced Tumor-Targeted Delivery of Antimicrobial Peptides.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Concentration Effects in Peptide-Lipid Bilayer Interactions: A Coarse-Grained Molecular Dynamics Study.The journal of physical chemistry. B · 2026Article
- Melittin Acts as a Radiosensitizer for Non-Small Cell Lung Cancer by Inhibiting the DNA Damage Repair System and Inducing Apoptosis.Yonsei medical journal · 2026Article
- From Membrane Composition to Antimicrobial Strategies: Experimental and Computational Approaches to AMP Design and Selectivity.Small (Weinheim an der Bergstrasse, Germany) · 2026Review
- Article
- Melittin-Loaded FeInternational journal of nanomedicine · 2026Article
- On the Effect of Melittin on Surface Properties of Erythrocyte and Mitochondrial Membranes.Membranes · 2025Article
- Elucidating the Impact of Red Blood Cell Membrane Components on Melittin-Induced Pore Formation with Molecular Dynamics Simulations.The journal of physical chemistry. B · 2025Article
- Antimicrobial Potential of Bee-Derived Products: Insights into Honey, Propolis and Bee Venom.Pathogens (Basel, Switzerland) · 2025Review
- Molecular dynamics study of the helix-to-disorder transition in short antimicrobial peptides from Urodacus yaschenkoi.European biophysics journal : EBJ · 2025Article
- The difference between MelP5 and melittin membrane poration.Scientific reports · 2025Article
- Article
- Molecular and energetic analysis of the interaction and specificity of Maximin 3 with lipid membranes: In vitro and in silico assessments.Protein science : a publication of the Protein Society · 2024Article
- Anticancer potentiality of Hottentotta saulcyi scorpion curd venom against breast cancer: an in vitro and in vivo study.Scientific reports · 2024Article
- Membrane Activity of Melittin and Magainin-I at Low Peptide-to-Lipid Ratio: Different Types of Pores and Translocation Mechanisms.Biomolecules · 2024Article
- Melittin can permeabilize membranes via large transient pores.Nature communications · 2024Article
- Analysis of risk factors for acute kidney injury in children with severe wasp stings.Pediatric nephrology (Berlin, Germany) · 2024Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Antimicrobial peptides (AMPs), as a key component of the immune defense systems of organisms, are a promising solution to the serious threat of drug-resistant bacteria to public health. As one of the most representative and extensively studied AMPs, melittin has exceptional broad-spectrum activities against microorganisms, including both Gram-positive and Gram-negative bacteria. Unfortunately, the action mechanism of melittin with bacterial membranes, especially the underlying physics of peptide-induced membrane poration behaviors, is still poorly understood, which hampers efforts to develop melittin-based drugs or agents for clinical applications. In this mini-review, we focus on recent advances with respect to the membrane insertion behavior of melittin mostly from a computational aspect. Membrane insertion is a prerequisite and key step for forming transmembrane pores and bacterial killing by melittin, whose occurrence is based on overcoming a high free-energy barrier during the transition of melittin molecules from a membrane surface-binding state to a transmembrane-inserting state. Here, intriguing simulation results on such transition are highlighted from both kinetic and thermodynamic aspects. The conformational changes and inter-peptide cooperation of melittin molecules, as well as melittin-induced disturbances to membrane structure, such as deformation and lipid extraction, are regarded as key factors influencing the insertion of peptides into membranes. The associated intermediate states in peptide conformations, lipid arrangements, membrane structure, and mechanical properties during this process are specifically discussed. Finally, potential strategies for enhancing the poration ability and improving the antimicrobial performance of AMPs are included as well.
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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.