ArticleToxins2013
Multiple membrane interactions and versatile vesicle deformations elicited by melittin.
Article in Toxins, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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
25 citing papers in PubMed, 42 citations in OpenAlex.
- Melittin-modified Paclitaxel Liposomes as a Synergistic Strategy for Anti-keloid Therapy.The AAPS journal · 2026Article
- High-Throughput Screening of FDA-Approved Drugs for Antibacterial and Antibiofilm Activities Against Multidrug-resistantACS omega · 2026Article
- On the Effect of Melittin on Surface Properties of Erythrocyte and Mitochondrial Membranes.Membranes · 2025Article
- Microneedle Assisted Melittin-Chondroitin Sulfate Administration for the Transdermal Therapy of Rheumatoid Arthritis.Advanced healthcare materials · 2025Article
- Antibacterial and anti-biofilm activities of Derazantinib (ARQ-087) against Staphylococcus aureus.Archives of microbiology · 2025Article
- Lipid vesicle-based molecular robots.Lab on a chip · 2024Review
- Liposome Deformation Induced by Membrane-Binding Peptides.Micromachines · 2023Article
- Article
- Repurposing Candesartan Cilexetil as Antibacterial Agent for MRSA Infection.Frontiers in microbiology · 2021Article
- Photo-initiated rupture of azobenzene micelles to enable the spectroscopic analysis of antimicrobial peptide dynamics.RSC advances · 2020Article
- The Effect of Bee Venom Peptides Melittin, Tertiapin, and Apamin on the Human Erythrocytes Ghosts: A Preliminary Study.Metabolites · 2020Article
- What Makes a Good Pore Former: A Study of Synthetic Melittin Derivatives.Biophysical journal · 2020Article
- Review
- Article
- Interspecies Bombolitins Exhibit Structural Diversity upon Membrane Binding, Leading to Cell Specificity.Biophysical journal · 2019Article
- Peptide-Lipid Interaction Sites Affect Vesicles' Responses to Antimicrobial Peptides.Biophysical journal · 2018Article
- The lipid mediator lysophosphatidic acid induces folding of disordered peptides with basic amphipathic character into rare conformations.Scientific reports · 2018Article
- Interactions between lipids and proteins are critical for organization of plasma membrane-ordered domains in tobacco BY-2 cells.Journal of experimental botany · 2018Article
- Effects of Peptide Charge, Orientation, and Concentration on Melittin Transmembrane Pores.Biophysical journal · 2018Article
- The novel antibiotic rhodomyrtone traps membrane proteins in vesicles with increased fluidity.PLoS pathogens · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Melittin induces various reactions in membranes and has been widely studied as a model for membrane-interacting peptide; however, the mechanism whereby melittin elicits its effects remains unclear. Here, we observed melittin-induced changes in individual giant liposomes using direct real-time imaging by dark-field optical microscopy, and the mechanisms involved were correlated with results obtained using circular dichroism, cosedimentation, fluorescence quenching of tryptophan residues, and electron microscopy. Depending on the concentration of negatively charged phospholipids in the membrane and the molecular ratio between lipid and melittin, melittin induced the "increasing membrane area", "phased shrinkage", or "solubilization" of liposomes. In phased shrinkage, liposomes formed small particles on their surface and rapidly decreased in size. Under conditions in which the increasing membrane area, phased shrinkage, or solubilization were mainly observed, the secondary structure of melittin was primarily estimated as an α-helix, β-like, or disordered structure, respectively. When the increasing membrane area or phased shrinkage occurred, almost all melittin was bound to the membranes and reached more hydrophobic regions of the membranes than when solubilization occurred. These results indicate that the various effects of melittin result from its ability to adopt various structures and membrane-binding states depending on the conditions.
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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.