ArticleScientific reports2016
Membrane Core-Specific Antimicrobial Action of Cathelicidin LL-37 Peptide Switches Between Pore and Nanofibre Formation.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
37 citing papers in PubMed, 1 synthesis or guideline pooled it, 73 citations in OpenAlex.
- Pooled it
- Apoptosis Modulation by LL-37: From Mitochondrial Cell Death to Prosurvival Signaling.International journal of molecular sciences · 2026Review
- Aggregation-State Dynamics Drive Double Cooperativity Between Antimicrobial Peptides LL-37 and HNP1.Angewandte Chemie (International ed. in English) · 2026Article
- Fever enhances host bacterial defence while limiting mitochondrial damage.Research square · 2026Article
- Integrating a cationic backbone with a hydrophobic core: A structure-function strategy for designing self-assembling antimicrobial peptides with enhanced activity.Zoological research · 2025Article
- Galectin-3: a novel antimicrobial host factor identified in goat nasal mucus.Veterinary research · 2025Article
- Exploring the Role of Tripeptides in Wound Healing and Skin Regeneration: A Comprehensive Review.International journal of medical sciences · 2025Review
- Recent advances in the therapeutic potential of cathelicidins.Frontiers in microbiology · 2024Review
- Resistance is futile: targeting multidrug-resistant bacteria withRSC chemical biology · 2023Review
- Article
- Vitamin D, Cellular Senescence and Chronic Kidney Diseases: What Is Missing in the Equation?Nutrients · 2023Review
- The role of bacterial transport systems in the removal of host antimicrobial peptides in Gram-negative bacteria.FEMS microbiology reviews · 2022Review
- Clostridioides difficile Modifies its Aromatic Compound Metabolism in Response to Amidochelocardin-Induced Membrane Stress.mSphere · 2022Article
- An Update on the Effects of Vitamin D on the Immune System and Autoimmune Diseases.International journal of molecular sciences · 2022Review
- Cathelicidin LL-37 in Health and Diseases of the Oral Cavity.Biomedicines · 2022Review
- Lipid tails modulate antimicrobial peptide membrane incorporation and activity.Biochimica et biophysica acta. Biomembranes · 2022Article
- The Role of Vitamin D in Supporting Health in the COVID-19 Era.International journal of molecular sciences · 2022Review
- Endogenous Peptide Inhibitors of HIV Entry.Advances in experimental medicine and biology · 2022Article
- Vitamin D as a Risk Factor for Multiple Sclerosis: Immunoregulatory or Neuroprotective?Frontiers in neurology · 2022Review
- The role of vitamin D in reducing SARS-CoV-2 infection: An update.International immunopharmacology · 2021Review
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 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane-disrupting antimicrobial peptides provide broad-spectrum defence against localized bacterial invasion in a range of hosts including humans. The most generally held consensus is that targeting to pathogens is based on interactions with the head groups of membrane lipids. Here we show that the action of LL-37, a human antimicrobial peptide switches the mode of action based on the structure of the alkyl chains, and not the head groups of the membrane forming lipids. We demonstrate that LL-37 exhibits two distinct interaction pathways: pore formation in bilayers of unsaturated phospholipids and membrane modulation with saturated phospholipids. Uniquely, the membrane modulation yields helical-rich fibrous peptide-lipid superstructures. Our results point at alternative design strategies for peptide antimicrobials.
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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.