ArticleBiophysical journal2011
Transmembrane pores formed by human antimicrobial peptide LL-37.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.
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Who cites it
89 citing papers in PubMed, 191 citations in OpenAlex.
- Vitamin D and antimicrobial peptides in skin health and disease: Mechanisms and therapeutic potential.Biochemistry and biophysics reports · 2026Review
- Overcoming LPS-mediated resistance in gram-negative pathogens: a review of LL-37 analogs and computational design strategies.Archives of microbiology · 2026Review
- Serine protease HtrA promotesScience advances · 2026Article
- Aggregation-State Dynamics Drive Double Cooperativity Between Antimicrobial Peptides LL-37 and HNP1.Angewandte Chemie (International ed. in English) · 2026Article
- Bacterial cell fate under stress: lipid remodeling and antimicrobial peptide attack.npj antimicrobials and resistance · 2026Article
- Heteroaggregation of Antimicrobial Peptides LL-37 and HNP‑1 Drives Cooperative Neutralization of Cytotoxicity.JACS Au · 2026Article
- From Membrane Composition to Antimicrobial Strategies: Experimental and Computational Approaches to AMP Design and Selectivity.Small (Weinheim an der Bergstrasse, Germany) · 2026Review
- Fever enhances host bacterial defence while limiting mitochondrial damage.Research square · 2026Article
- Predicting peptide orientation in membrane interactions: a review on transmembrane and surface-bound states.European biophysics journal : EBJ · 2026Review
- Overview of dendrimers as promising drug delivery systems with insight into anticancer and anti-microbial applications.International journal of pharmaceutics: X · 2025Review
- Bactericidal activity of mammalian histones is caused by large membrane pore formation.Cell reports · 2025Article
- Phage-Encoded Antimicrobial Peptide gp28 Demonstrates LL-37-Like Antimicrobial Activity Against Multidrug-ResistantPHAGE (New Rochelle, N.Y.) · 2025Article
- Segment-Based Peptide Design Reveals the Importance of N-Terminal High Cationicity for Antimicrobial Activity Against Gram-Negative Pathogens.Probiotics and antimicrobial proteins · 2025Article
- Role of innate host defense proteins in oral cancerogenesis.Periodontology 2000 · 2024Review
- Antimicrobial Activity of Positively Charged Oligopeptides with Theoretical High α-Helix Content againstInternational journal of molecular sciences · 2024Article
- Recent Advances in Vitamin D3 Intervention to EradicateJournal of multidisciplinary healthcare · 2024Review
- Lipid-Centric Approaches in Combating Infectious Diseases: Antibacterials, Antifungals and Antivirals with Lipid-Associated Mechanisms of Action.Antibiotics (Basel, Switzerland) · 2023Review
- The Functionality of Membrane-Inserting Proteins and Peptides: Curvature Sensing, Generation, and Pore Formation.The Journal of membrane biology · 2023Review
- Design, synthesis, and characterization of non-hemolytic antimicrobial peptides related to human cathelicidin LL-37.RSC advances · 2023Article
- Electrochemiluminescence Imaging of Liposome Permeabilization by an Antimicrobial Peptide: Melittin.Chemical & biomedical imaging · 2023Article
29 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Human LL-37 is a multifunctional cathelicidin peptide that has shown a wide spectrum of antimicrobial activity by permeabilizing microbial membranes similar to other antimicrobial peptides; however, its molecular mechanism has not been clarified. Two independent experiments revealed LL-37 bound to membranes in the α-helical form with the axis lying in the plane of membrane. This led to the conclusion that membrane permeabilization by LL-37 is a nonpore carpet-like mechanism of action. Here we report the detection of transmembrane pores induced by LL-37. The pore formation coincided with LL-37 helices aligning approximately normal to the plane of the membrane. We observed an unusual phenomenon of LL-37 embedded in stacked membranes, which are commonly used in peptide orientation studies. The membrane-bound LL-37 was found in the normal orientation only when the membrane spacing in the multilayers exceeded its fully hydrated value. This was achieved by swelling the stacked membranes with excessive water to a swollen state. The transmembrane pores were detected and investigated in swollen states by means of oriented circular dichroism, neutron in-plane scattering, and x-ray lamellar diffraction. The results are consistent with the effect of LL-37 on giant unilamellar vesicles. The detected pores had a water channel of radius 23-33 Å. The molecular mechanism of pore formation by LL-37 is consistent with the two-state model exhibited by magainin and other small pore-forming peptides. The discovery that peptide-membrane interactions in swollen states are different from those in less hydrated states may have implications for other large membrane-active peptides and proteins studied in stacked membranes.
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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.