ReviewBiochimica et biophysica acta2014
Membrane-active peptides: binding, translocation, and flux in lipid vesicles.
Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed.
- Is the Bilayer Insertion of the Peptide KALP23 Under Kinetic or Thermodynamic Control?The Journal of membrane biology · 2026Article
- Lipidated peptides and the limits of chemical control.Frontiers in chemistry · 2026Article
- A unified model of transient poration induced by antimicrobial peptides.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Role of Flexibility in the Bioactivity of Short α-Helical Antimicrobial Peptides.Antibiotics (Basel, Switzerland) · 2025Review
- Expression and purification of epinecidin-1 variant (Ac-Var-1) by acid cleavage.Applied microbiology and biotechnology · 2024Article
- Bio-Membrane Internalization Mechanisms of Arginine-Rich Cell-Penetrating Peptides in Various Species.Membranes · 2022Article
- Novel Antimicrobial Peptides from a Cecropin-Like Region of Heteroscorpine-1 fromMolecules (Basel, Switzerland) · 2021Article
- Towards a Quantitative Understanding of Protein-Lipid Bilayer Interactions at the Single Molecule Level: Opportunities and Challenges.The Journal of membrane biology · 2021Review
- The Antibiotic Peptide Daptomycin Functions by Reorganizing the Membrane.The Journal of membrane biology · 2021Review
- Electrostatic effects in saturation of membrane binding of cationic cell-penetrating peptide.European biophysics journal : EBJ · 2021Article
- Using fluorescence microscopy to shed light on the mechanisms of antimicrobial peptides.Future medicinal chemistry · 2019Review
- Article
- Charged N-terminus of Influenza Fusion Peptide Facilitates Membrane Fusion.International journal of molecular sciences · 2018Article
- Fluorescence Imaging of Disrupted Interfaces between Liquid-Ordered and Liquid-Disordered Domains by a Flavin-Labeled PNA Duplex.ACS omega · 2017Article
- Coarse-grained simulations of hemolytic peptide δ-lysin interacting with a POPC bilayer.Biochimica et biophysica acta · 2016Article
- Charge Distribution Fine-Tunes the Translocation of α-Helical Amphipathic Peptides across Membranes.Biophysical journal · 2016Article
- Vesicle Leakage Reflects the Target Selectivity of Antimicrobial Lipopeptides from Bacillus subtilis.Biophysical journal · 2015Article
- Cell-penetrating antimicrobial peptides - prospectives for targeting intracellular infections.Pharmaceutical research · 2015Article
- gH625: a milestone in understanding the many roles of membranotropic peptides.Biochimica et biophysica acta · 2015Review
- Lysylated phospholipids stabilize models of bacterial lipid bilayers and protect against antimicrobial peptides.Biochimica et biophysica acta · 2014Article
Corrections and comments
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Authors and funding
1 author.
Funding
Abstract
Recently, new and improved methods have been developed to measure translocation of membrane-active peptides (antimicrobial, cytolytic, and amphipathic cell-penetrating peptides) across lipid bilayer membranes. The hypothesis that translocation of membrane-active peptides across a lipid bilayer is determined by the Gibbs energy of insertion of the peptide into the bilayer is re-examined in the light of new experimental tests. The original hypothesis and its motivation are first revisited, examining some of the specific predictions that it generated, followed by the results of the initial tests. Translocation is understood as requiring two previous steps: binding and insertion in the membrane. The problem of peptide binding to membranes, its prediction, measurement, and calculation are addressed. Particular attention is given to understanding the reason for the need for amphipathic structures in the function of membrane-active peptides. Insertion into the membrane is then examined. Hydrophobicity scales are compared, and their influence on calculations is discussed. The relation between translocation and graded or all-or-none peptide-induced flux from or into lipid vesicles is also considered. Finally, the most recent work on translocation is examined, both experimental and from molecular dynamics simulations. This article is part of a Special Issue entitled: Interfacially Active Peptides and Proteins. Guest Editors: William C. Wimley and Kalina Hristova.
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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.