ArticleBiophysical journal2018
Effects of Peptide Charge, Orientation, and Concentration on Melittin Transmembrane Pores.
Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 49 citations in OpenAlex.
- The Role of Flexibility in the Bioactivity of Short α-Helical Antimicrobial Peptides.Antibiotics (Basel, Switzerland) · 2025Review
- Melittin can permeabilize membranes via large transient pores.Nature communications · 2024Article
- Structural Determinants of Peptide Nanopore Formation.ACS nano · 2024Article
- Brain-targeted drug delivery - nanovesicles directed to specific brain cells by brain-targeting ligands.Journal of nanobiotechnology · 2024Review
- Structure, Function, and Physicochemical Properties of Pore-forming Antimicrobial Peptides.Current pharmaceutical biotechnology · 2024Review
- Revisiting edible insects as sources of therapeutics and drug delivery systems for cancer therapy.Frontiers in pharmacology · 2024Review
- Antiviral attributes of bee venom as a possible therapeutic approach against SARS-CoV-2 infection.Future virology · 2023Review
- The role of peptides in reversing chemoresistance of breast cancer: current facts and future prospects.Frontiers in pharmacology · 2023Review
- Organizations of melittin peptides after spontaneous penetration into cell membranes.Biophysical journal · 2022Article
- The reduced-charge melittin analogue MelP5 improves the transfection of non-viral DNA nanoparticles.Journal of peptide science : an official publication of the European Peptide Society · 2022Article
- Integrated Design of a Membrane-Lytic Peptide-Based Intravenous Nanotherapeutic Suppresses Triple-Negative Breast Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Single-molecule phospholipase ABiophysical journal · 2022Article
- Predicting Membrane-Active Peptide Dynamics in Fluidic Lipid Membranes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Switching Cytolytic Nanopores into Antimicrobial Fractal Ruptures by a Single Side Chain Mutation.ACS nano · 2021Article
- Lipid interactions of an actinoporin pore-forming oligomer.Biophysical journal · 2021Article
- Tuning of a Membrane-Perforating Antimicrobial Peptide to Selectively Target Membranes of Different Lipid Composition.The Journal of membrane biology · 2021Article
- In Silico Prediction of the Binding, Folding, Insertion, and Overall Stability of Membrane-Active Peptides.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Opposite Regulatory Effects of Immobilized Cations on the Folding Vs. Assembly of Melittin.Frontiers in chemistry · 2021Article
- Using Simulation to Understand the Role of Titration on the Stability of a Peptide-Lipid Bilayer Complex.Langmuir : the ACS journal of surfaces and colloids · 2020Article
- Dual-Modified Liposome for Targeted and Enhanced Gene Delivery into Mice Brain.The Journal of pharmacology and experimental therapeutics · 2020Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Melittin is a short cationic peptide that exerts cytolytic effects on bacterial and eukaryotic cells. Experiments suggest that in zwitterionic membranes, melittin forms transmembrane toroidal pores supported by four to eight peptides. A recently constructed melittin variant with a reduced cationic charge, MelP5, is active at 10-fold lower concentrations. In previous work, we performed molecular dynamics simulations on the microsecond timescale to examine the supramolecular pore structure of a melittin tetramer in zwitterionic and partially anionic membranes. We now extend that study to include the effects of peptide charge, initial orientation, and number of monomers on the pore formation and stabilization processes. Our results show that parallel transmembrane orientations of melittin and MelP5 are more consistent with experimental data. Whereas a MelP5 parallel hexamer forms a large stable pore during the 5-μs simulation time, a melittin hexamer and an octamer are not fully stable, with several monomers dissociating during the simulation time. Interaction-energy analysis shows that this difference in behavior between melittin and MelP5 is not due to stronger electrostatic repulsion between neighboring melittin peptides but to peptide-lipid interactions that disfavor the isolated MelP5 transmembrane monomer. The ability of melittin monomers to diffuse freely in the 1,2-dimyristoyl-SN-glycero-3-phosphocholine membrane leads to dynamic pores with varying molecularity.
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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.