ReviewEuropean biophysics journal : EBJ2011
A lipocentric view of peptide-induced pores.
Review in European biophysics journal : EBJ, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- Combating Bacterial Infections with Vitamin D-Induced Antimicrobial Peptides.Advances in experimental medicine and biology · 2026Review
- Structural pores not required: Antimicrobial peptides induce ion permeabilization of lipid membranes through transient water channels.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Advances in Antimicrobial Peptides: Mechanisms, Design Innovations, and Biomedical Potential.Molecules (Basel, Switzerland) · 2025Review
- Article
- Combating antibiotic resistance in a one health context: a plethora of frontiers.One health outlook · 2024Review
- Alteration of Average Thickness of Lipid Bilayer by Membrane-Deforming Inclusions.Biomolecules · 2023Article
- Initiation and evolution of pores formed by influenza fusion peptides probed by lysolipid inclusion.Biophysical journal · 2023Article
- Article
- Anti-Virulence Potential of a Chionodracine-Derived Peptide against Multidrug-ResistantInternational journal of molecular sciences · 2022Article
- A mutation in the S6 segment of the KvAP channel changes the secondary structure and alters ion channel activity in a lipid bilayer membrane.Amino acids · 2022Article
- Effects of cholesterol on the anionic magnetite nanoparticle-induced deformation and poration of giant lipid vesicles.RSC advances · 2022Article
- Review
- Recent developments in the kinetics of ruptures of giant vesicles under constant tension.RSC advances · 2021Review
- A photoswitchable helical peptide with light-controllable interface/transmembrane topology in lipidic membranes.iScience · 2021Article
- Latest developments on the mechanism of action of membrane disrupting peptides.Biophysics reports · 2021Article
- Pore formation in regulated cell death.The EMBO journal · 2020Review
- Location of Peptide-Induced Submicron Discontinuities in the Membranes of Vesicles Using ImageJ.Journal of fluorescence · 2020Article
- Elastic deformations mediate interaction of the raft boundary with membrane inclusions leading to their effective lateral sorting.Scientific reports · 2020Article
- A Multiomics Approach Unravels New Toxins With PossibleFrontiers in pharmacology · 2020Article
- Effects of electrically-induced constant tension on giant unilamellar vesicles using irreversible electroporation.European biophysics journal : EBJ · 2019Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although lipid membranes serve as effective sealing barriers for the passage of most polar solutes, nonmediated leakage is not completely improbable. A high activation energy normally keeps unassisted bilayer permeation at a very low frequency, but lipids are able to self-organize as pores even in peptide-free and protein-free membranes. The probability of leakage phenomena increases under conditions such as phase coexistence, external stress or perturbation associated to binding of nonlipidic molecules. Here, we argue that pore formation can be viewed as an intrinsic property of lipid bilayers, with strong similarities in the structure and mechanism between pores formed with participation of peptides, lipidic pores induced by different types of stress, and spontaneous transient bilayer defects driven by thermal fluctuations. Within such a lipocentric framework, amphipathic peptides are best described as pore-inducing rather than pore-forming elements. Active peptides bound to membranes can be understood as a source of internal surface tension which facilitates pore formation by diminishing the high activation energy barrier. This first or immediate action of the peptide has some resemblance to catalysis. However, the presence of membrane-active peptides has the additional effect of displacing the equilibrium towards the pore-open state, which is then maintained over long times, and reducing the size of initial individual pores. Thus, pore-inducing peptides, regardless of their sequence and oligomeric organization, can be assigned a double role of increasing the probability of pore formation in membranes to high levels as well as stabilizing these pores after they appear.
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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.