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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
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Utility 2
pubmed Jan 18, 2009

[Characteristics of the main groups of human host-defensive peptides].

Lapis. Károly K

The paper reviews three main groups of human antimicrobial peptides—defensins, cathelicidins (including LL‑37), and histatins—showing they do more than kill microbes. They also help regulate the immune system and may be linked to disease when they don’t work right, which is why drug companies are interested.

Utility 2
pubmed Mar 15, 2004

The human cationic peptide LL-37 induces activation of the extracellular signal-regulated kinase and p38 kinase pathways in primary human monocytes.

Bowdish. Dawn M E DM; Davidson. Donald J DJ; Speert. David P DP; Hancock. Robert E W RE

LL-37 is a natural protein that can turn on specific signaling pathways (ERK1/2 and p38) in human monocytes, leading these immune cells to release the inflammatory signal IL‑8. This effect is stronger when another growth factor (GM‑CSF) is present, but it doesn’t happen in B or T cells. The peptide works without the previously‑thought receptor, suggesting other ways it can influence immunity.

Utility 2
pubmed May 1, 2005

Antimicrobial protein hCAP18/LL-37 is highly expressed in breast cancer and is a putative growth factor for epithelial cells.

Heilborn. Johan D JD; Nilsson. Margareta Frohm MF; Jimenez. Clara I Chamorro CI; Sandstedt. Bengt B;...

The study found that the antimicrobial peptide LL‑37, normally part of our innate immune system, is found in high amounts inside breast cancer cells and actually makes those cells grow faster, not slower. Adding synthetic LL‑37 to lab-grown epithelial cells boosted their division, and cells engineered to produce LL‑37 also multiplied more. This suggests LL‑37 could act like a growth factor for certain tumors rather than fighting them.

Utility 2
pubmed Jul 1, 2005

Neisseria gonorrhoeae downregulates expression of the human antimicrobial peptide LL-37.

Bergman. Peter P; Johansson. Linda L; Asp. Vendela V; Plant. Laura L; Gudmundsson. Gudmundur H GH; J...

The study shows that the human antimicrobial peptide LL‑37 can kill the gonorrhea bacteria in lab tests, but the live pathogen can actually lower the amount of LL‑37 that our own cells make, especially the harmful strains. This means the bacteria have a trick to dodge this natural defense, and dead bacteria don’t cause the same effect.

Utility 2
pubmed Oct 1, 2005

Transient cutaneous adenoviral gene therapy with human host defense peptide hCAP-18/LL-37 is effective for the treatment of burn wound infections.

Jacobsen. F F; Mittler. D D; Hirsch. T T; Gerhards. A A; Lehnhardt. M M; Voss. B B; Steinau. H U HU;...

A study in rats showed that delivering the natural antimicrobial peptide LL‑37 via a virus (adenovirus) into burn wounds dramatically cut bacterial infection, far more than applying the synthetic peptide directly. While the virus‑based method worked great in the lab, it isn’t something most people can do at home, and the plain peptide still had some modest effect.

Utility 2
pubmed 2005

Effect of antibacterial cathelicidin peptide CAP18/LL-37 on sepsis in neonatal rats.

Fukumoto. Koji K; Nagaoka. Isao I; Yamataka. Atsuyuki A; Kobayashi. Hiroyuki H; Yanai. Toshihiro T;...

In newborn rats with a sepsis-like infection, the natural antimicrobial peptide LL‑37 helped some animals survive, especially when given at the same time as the infection or in low amounts later. However, giving too much LL‑37 after the infection actually made things worse, and the study was done only in rat pups, not people.

Utility 2
pubmed Feb 1, 2005

Augmentation of the bactericidal activities of human cathelicidin CAP18/LL-37-derived antimicrobial peptides by amino acid substitutions.

Nagaoka. I I; Kuwahara-Arai. K K; Tamura. H H; Hiramatsu. K K; Hirata. M M

Scientists tweaked a natural human antimicrobial peptide called LL-37 and found that swapping a few building blocks made it much better at killing a wide range of bacteria, including tough strains like MRSA. The most effective version, named 18‑mer LLKKK, was especially good at breaking bacterial membranes.

Utility 2
pubmed Apr 27, 2006

Involvement of the antimicrobial peptide LL-37 in human atherosclerosis.

Edfeldt. Kristina K; Agerberth. Birgitta B; Rottenberg. Martin E ME; Gudmundsson. Gudmundur H GH; Wa...

The study found that the immune peptide LL‑37 is much higher in clogged arteries and is made by immune cells there. It can turn on other molecules that attract more immune cells, which might worsen artery disease. So, raising LL‑37 levels isn’t clearly a good move for heart health.

Utility 2
pubmed Oct 15, 2006

Release of LL-37 by activated human Vgamma9Vdelta2 T cells: a microbicidal weapon against Brucella suis.

Dudal. Sherri S; Turriere. Chrystell C; Bessoles. Stephanie S; Fontes. Pascaline P; Sanchez. Fran&#x...

When a special type of immune cell (Vγ9Vδ2 T cell) gets activated, it releases a natural antimicrobial protein called LL‑37, which can kill the bacteria Brucella suis. This shows that LL‑37 is part of the body’s own weaponry against certain infections.

Utility 2
pubmed 2006

Immunomodulatory properties of defensins and cathelicidins.

Bowdish. D M E DM; Davidson. D J DJ; Hancock. R E W RE

LL-37 is a natural peptide that helps the body fight infections and control the immune system. It can kill microbes directly, attract immune cells, help wounds heal, and influence how the adaptive immune system works. People who lack LL-37 get sick more often, and scientists think it could become a new kind of medicine, but we don't yet know how to use it safely.

Utility 2
pubmed Aug 1, 2005

Expression and modulation of LL-37 in normal human keratinocytes, HaCaT cells, and inflammatory skin diseases.

Kim. Ji Eun JE; Kim. Beom Joon BJ; Jeong. Mi Sook MS; Seo. Seong Jun SJ; Kim. Myeung Nam MN; Hong. C...

The study shows that the skin’s natural antimicrobial peptide LL‑37 is made by normal skin cells but not by a common lab‑grown skin cell line, and its production goes up after UV‑B light or bacterial components, especially in psoriasis‑affected skin.

Utility 2
pubmed Dec 9, 2005

Apoptosis of airway epithelial cells: human serum sensitive induction by the cathelicidin LL-37.

Lau. Y Elaine YE; Bowdish. Dawn M E DM; Cosseau. Celine C; Hancock. Robert E W RE; Davidson. Donald...

The study shows that the human peptide LL‑37 can kill airway lining cells by triggering apoptosis, but this harmful effect is stopped by components in human blood, especially HDL, while animal serum doesn’t help. This means LL‑37 might be useful against infections in places with low blood protein levels, but could also damage cells if not properly buffered by human serum factors.

Utility 2
pubmed Feb 28, 2006

Expression and purification of a recombinant LL-37 from Escherichia coli.

Moon. Ja-Young JY; Henzler-Wildman. Katherine A KA; Ramamoorthy. A A

Scientists figured out a lab method to make the immune‑boosting peptide LL‑37 in bacteria and pull it out in a pure form, even adding special nitrogen labels for detailed studies. The process uses a GST tag, a specific enzyme cut, and high‑pressure liquid chromatography, giving modest amounts of peptide. For DIY bio‑enthusiasts it shows that making LL‑37 is possible, but the steps need a fully equipped molecular‑biology setup, so it isn’t a quick home‑brew recipe.

Utility 2
pubmed 2005

Expression of mRNA and proteins for toll-like receptors, associated molecules, defensins and LL-37 by SRIK-NKL, a CD8+ NK/T cell line.

Srivastava. Maya D MD; Srivastava. B I S BI

Researchers found that a lab-grown NK/T cell line can make the antimicrobial peptide LL‑37 and many toll‑like receptors, and that when these cells encounter live bacteria they multiply and release more immune signaling molecules. This shows that immune cells naturally produce LL‑37 as part of their defense, but the study doesn’t give direct tips on how to use LL‑37 for health purposes.

Utility 2
pubmed Jun 1, 2005

Candidacidal effects of two antimicrobial peptides: histatin 5 causes small membrane defects, but LL-37 causes massive disruption of the cell membrane.

den Hertog. Alice L AL; van Marle. Jan J; van Veen. Henk A HA; Van't Hof. Wim W; Bolscher. Jan G M J...

The study shows that the human peptide LL-37 smashes the Candida fungus cell membrane into pieces, while another saliva peptide, histatin 5, makes tiny holes but still kills the fungus by leaking out its building blocks.

Utility 2
pubmed 2005

Interaction and cellular localization of the human host defense peptide LL-37 with lung epithelial cells.

Lau. Y Elaine YE; Rozek. Annett A; Scott. Monisha G MG; Goosney. Danika L DL; Davidson. Donald J DJ;...

The study shows that the human peptide LL‑37 can enter lung cells, move toward the cell’s center, and likely interacts with two different cell surface receptors. This internal uptake depends on normal cell‑eating processes and the cell’s internal transport system, not on actin filaments.

Utility 2
pubmed Jun 17, 2005

Human endogenous antibiotic LL-37 stimulates airway epithelial cell proliferation and wound closure.

Shaykhiev. Renat R; Beisswenger. Christoph C; Kändler. Kerstin K; Senske. Judith J; Püchne...

The study shows that the natural human peptide LL‑37 can help airway cells grow and close wounds in lab dishes, working at low microgram‑per‑millilitre levels, but only when serum is present. It does this by activating growth‑related pathways like the epidermal growth factor receptor and MAPK. This is an early‑stage, cell‑culture finding, not a tested human treatment.

Utility 2
pubmed Jun 15, 2005

Synergistic effect of antibacterial agents human beta-defensins, cathelicidin LL-37 and lysozyme against Staphylococcus aureus and Escherichia coli.

Chen. Xuejun X; Niyonsaba. François F; Ushio. Hiroko H; Okuda. Daiju D; Nagaoka. Isao I; Ikeda....

The study shows that the skin’s natural antimicrobial peptides—human beta‑defensins, LL‑37, and lysozyme—work better together than alone, especially against Staphylococcus aureus, and that a slightly acidic environment (pH 4.6) makes most of them more potent, though LL‑37 itself isn’t boosted by acid. This synergy is less clear for E. coli.

Utility 2
pubmed Oct 1, 2004

Bacterial products increase expression of the human cathelicidin hCAP-18/LL-37 in cultured human sinus epithelial cells.

Nell. Marja J MJ; Tjabringa. G Sandra GS; Vonk. Marcel J MJ; Hiemstra. Pieter S PS; Grote. Jan J JJ

The study shows that bacterial molecules like lipopolysaccharide (LPS) from gram‑negative bacteria and lipoteichoic acid (LTA) from gram‑positive bacteria can make sinus cells produce more of the natural antimicrobial peptide LL‑37, as well as more mucus and an inflammation signal (IL‑8). This was seen in a lab dish, not in people.

Utility 2
pubmed 2004

Histone-deacetylase inhibitors induce the cathelicidin LL-37 in gastrointestinal cells.

Schauber. Jürgen J; Iffland. Konrad K; Frisch. Susanne S; Kudlich. Theodor T; Schmausser. Bernd...

The study shows that chemicals called HDAC inhibitors, like the natural compound butyrate (found in high‑fiber foods), can turn on the production of the antimicrobial peptide LL‑37 in colon, stomach and liver cancer cells. This effect depends on changes to proteins that control gene activity and needs a specific cell signaling pathway. While it hints that boosting butyrate could enhance gut immunity, the work was done in cell lines, not people, so direct recommendations are limited.