ArticleBiochemistry2008
NMR structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecylphosphocholine micelles.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
92 citing papers in PubMed, 180 citations in OpenAlex.
- Article
- β-Amyloid (Aβ) and Human Cathelicidin LL-37: Two Sides of the Same Coin?International journal of molecular sciences · 2026Review
- Overcoming LPS-mediated resistance in gram-negative pathogens: a review of LL-37 analogs and computational design strategies.Archives of microbiology · 2026Review
- Bacterial cell fate under stress: lipid remodeling and antimicrobial peptide attack.npj antimicrobials and resistance · 2026Article
- Host Defense Antimicrobial Peptides (HDPs) as Regulators of Hemostasis and Vascular Biology.Biomolecules · 2026Review
- Species-dependent susceptibility of enterococci to bovine cathelicidin BMAP-28 and its relationship to membrane fatty acid composition.Frontiers in microbiology · 2026Article
- Potential Antiphotoaging Effect of Human Cathelicidin LL-37 Fragments and KR-12 Analogs on UVB-Induced HaCaT Cells and UVA-Induced HDF Cells.ACS omega · 2025Article
- Antimicrobial Peptides of the Cathelicidin Family: Focus on LL-37 and Its Modifications.International journal of molecular sciences · 2025Review
- Simultaneous assessment of membrane bilayer structure and drug insertion byBiophysical journal · 2025Article
- LL-37: Structures, Antimicrobial Activity, and Influence on Amyloid-Related Diseases.Biomolecules · 2024Review
- Structure-based mechanisms of 2'3'-cGAMP intercellular transport in the cGAS-STING immune pathway.Trends in immunology · 2023Review
- Design, synthesis, and characterization of non-hemolytic antimicrobial peptides related to human cathelicidin LL-37.RSC advances · 2023Article
- The role of bacterial transport systems in the removal of host antimicrobial peptides in Gram-negative bacteria.FEMS microbiology reviews · 2022Review
- Regulation of LL-37 in Bone and Periodontium Regeneration.Life (Basel, Switzerland) · 2022Review
- Metal-Ion Interactions with Dodecapeptide Fragments of Human Cationic Antimicrobial Protein LL-37 [hCAP(134-170)].The journal of physical chemistry. B · 2022Article
- Single-Cell Analysis of the Antimicrobial and Bactericidal Activities of the Antimicrobial Peptide Magainin 2.Microbiology spectrum · 2022Article
- Article
- Atomic-Resolution Structures and Mode of Action of Clinically Relevant Antimicrobial Peptides.International journal of molecular sciences · 2022Review
- Renovation as innovation: Repurposing human antibacterial peptide LL-37 for cancer therapy.Frontiers in pharmacology · 2022Review
- Structure and Activity of a Selective Antibiofilm Peptide SK-24 Derived from the NMR Structure of Human Cathelicidin LL-37.Pharmaceuticals (Basel, Switzerland) · 2021Article
32 more citing papers are in PubMed but not listed here.
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 3 institutions in 2 countries.
Funding
Abstract
LL-37 is the only cathelicidin-derived polypeptide found in humans. Its eclectic function makes this peptide one of the most intriguing chemical defense agents, with crucial roles in moderating inflammation, promoting wound healing, and boosting the human immune system. LL-37 kills both prokaryotic and eukaryotic cells through physical interaction with cell membranes. In order to study its active conformation in membranes, we have reconstituted LL-37 into dodecylphosphocholine (DPC) micelles and determined its three-dimensional structure. We found that, under our experimental conditions, this peptide adopts a helix-break-helix conformation. Both the N- and C-termini are unstructured and solvent exposed. The N-terminal helical domain is more dynamic, while the C-terminal helix is more solvent protected and structured (high density of NOEs, slow H/D exchange). When it interacts with DPC, LL-37 is adsorbed on the surface of the micelle with the hydrophilic face exposed to the water phase and the hydrophobic face buried in the micelle hydrocarbon region. The break between the helices is positioned at K12 and is probably stabilized by a hydrophobic cluster formed by I13, F17, and I20 in addition to a salt bridge between K12 and E16. These results support the proposed nonpore carpet-like mechanism of action, in agreement with the solid-state NMR studies, and pave the way for understanding the function of the mature LL-37 at the atomic level.
Indexed as
Identifiers
What OpenQuestion holds
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.