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LL-37

Cathelicidin, hCAP-18, FALL-39, CAP-18

An antimicrobial peptide of the cathelicidin family that provides innate immune defense by killing pathogens and modulating inflammation and wound healing.

Quick Stats
Studies 2230
Trials 95
Formula C205H340N60O53
Overview Studies 2230 Clinical Trials 95
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pubmed Apr 1, 2007

Low plasma levels of the protein pro-LL-37 as an early indication of severe disease in patients with chronic neutropenia.

Karlsson. Jenny J; Carlsson. Göran G; Ramme. Kim Göransdotter KG; Hägglund. Hans H; F...

The study measured a protein called pro‑LL‑37 in the blood of people with different kinds of chronic low white‑blood‑cell counts. It found that those with the most severe genetic form had almost none, while other types had normal or changing levels. This is mainly a diagnostic clue for a rare disease, not a health hack for everyday performance or longevity.

pubmed 2007

The density of negative charge in the cell wall influences two-component signal transduction in Bacillus subtilis.

Hyyryläinen. Hanne-Leena HL; Pietiäinen. Milla M; Lundén. Tuula T; Ekman. Anna A; Gar...

The study looks at how changing the electric charge on the surface of a common bacteria (Bacillus subtilis) affects the bacteria’s internal stress‑sensing systems, especially when exposed to the antimicrobial peptide LL‑37. It shows that making the cell wall more negatively charged flips the activity of several signaling pathways, but this is a basic microbiology finding and doesn’t translate into any direct health or performance advice for people.

pubmed Sep 25, 2006

Lipopolysaccharide from Escherichia coli induces the expression of vascular endothelial growth factor via toll-like receptor 4 in human limbal fibroblasts.

Rodríguez-Martínez. Sandra S; Cancino-Diaz. Mario E ME; Miguel. Pedroza-Seres PS; Cancino-...

The study shows that bacterial components (LPS) can make eye‑surface cells produce a blood‑vessel growth factor (VEGF) through a receptor called TLR4, but it does not affect the antimicrobial peptide LL‑37. This is mainly about eye inflammation, not something you can apply to general health or performance.

pubmed 2005

Cationic antimicrobial peptide resistance in Neisseria meningitidis.

Tzeng. Yih-Ling YL; Ambrose. Karita D KD; Zughaier. Susu S; Zhou. Xiaoliu X; Miller. Yoon K YK; Shaf...

This study looks at how the disease‑causing bacteria Neisseria meningitidis avoids being killed by the natural antimicrobial peptide LL‑37. It finds that the bacteria use a drug‑pumping system and chemical changes to its outer membrane to stay resistant, but the work doesn’t give any tips for using LL‑37 in humans or for health‑optimizing protocols.

pubmed 2001

RL-37, an alpha-helical antimicrobial peptide of the rhesus monkey.

Zhao. C C; Nguyen. T T; Boo. L M LM; Hong. T T; Espiritu. C C; Orlov. D D; Wang. W W; Waring. A A; L...

Rhesus monkey bone marrow expresses a cathelicidin whose C-terminal domain comprises a 37-residue alpha-helical peptide (RL-37) that resembles human LL-37. Like its human counterpart, RL-37 rapidly permeabilized the membranes of Escherichia coli ML-35p and lysed liposomes that simulated bacterial membranes. When tested in media whose NaCl concentrations approximated those of extracellular fluids, RL-37 was considerably more active than LL-37 against staphylococci. Whereas human LL-37 contains five acidic residues and has a net charge of +6, rhesus RL-37 has only two acidic residues and a net charge of +8. Speculating that the multiple acidic residues of human LL-37 reduced its efficacy against staphylococci, we made a peptide (LL-37 pentamide) in which each aspartic acid of LL-37 was replaced by an asparagine and each glutamic acid was replaced by a glutamine. LL-37 pentamide's antistaphylococcal activity was substantially greater than that of LL-37. Thus, although the precursor of LL-37 is induced in human skin keratinocytes by injury or inflammation, its insufficiently cationic antimicrobial domain may contribute to the success of staphylococci in colonizing and infecting human skin.