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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, 2013

The antimicrobial peptide LL-37 induces synthesis and release of cysteinyl leukotrienes from human eosinophils--implications for asthma.

Sun. J J; Dahlén. B B; Agerberth. B B; Haeggström. J Z JZ

The study shows that the natural antimicrobial peptide LL‑37 can activate eosinophils, the white‑blood cells that drive asthma attacks, causing them to release inflammation‑triggering molecules called cysteinyl leukotrienes and eosinophil cationic protein. This effect is stronger when the cells are already primed by asthma‑related signals or come from people with asthma. In short, LL‑37 may worsen airway inflammation rather than help it.

Utility 2
pubmed Jul 24, 2013

Boosting innate immunity: development and validation of a cell-based screening assay to identify LL-37 inducers.

Nylén. Frank F; Miraglia. Erica E; Cederlund. Andreas A; Ottosson. Håkan H; Strömberg...

Scientists created a lab test that can spot chemicals that make cells produce more of the immune peptide LL‑37, which helps protect against infections. They used the test to screen existing drugs and found five new compounds that boost LL‑37, but they haven’t tested them in people yet.

Utility 2
pubmed Feb 3, 2014

Fungicidal mechanisms of cathelicidins LL-37 and CATH-2 revealed by live-cell imaging.

Ordonez. Soledad R SR; Amarullah. Ilham H IH; Wubbolts. Richard W RW; Veldhuizen. Edwin J A EJ; Haag...

The study shows that the human peptide LL‑37 can quickly kill the fungus Candida albicans by punching holes in its cell membrane, but it’s not as fast or powerful as a similar chicken peptide called CATH‑2. All three peptides work differently, and LL‑37’s action doesn’t need the fungus’s energy supply.

Utility 2
pubmed Dec 28, 2012

Effect of antimicrobial peptides derived from human cathelicidin LL-37 on Entamoeba histolytica trophozoites.

Rico-Mata. Rosa R; De Leon-Rodriguez. Luis M LM; Avila. Eva E EE

The study found that the human antimicrobial peptide LL‑37 and three shorter versions (KR‑12, KR‑20, KS‑30) can kill the gut parasite Entamoeba histolytica in lab tests, with KR‑20 being the strongest. However, the peptides work only at relatively high concentrations (10‑50 µM) and the parasite’s enzymes can break them down, so they aren’t ready for practical self‑use yet.

Utility 2
pubmed Feb 8, 2013

Salivary concentration of free LL-37 in edentulism, chronic periodontitis and healthy periodontium.

Davidopoulou. Sotiria S; Diza. Eudoxia E; Sakellari. Dimitra D; Menexes. George G; Kalfas. Sotirios...

The study found that people with healthy gums have the most LL‑37, an antimicrobial peptide, in their saliva, while those with gum disease have less, and people without teeth have the least. Women with healthy gums showed slightly higher levels than men. This suggests that keeping your teeth and gums intact may help maintain natural oral defenses.

Utility 2
pubmed Aug 4, 2014

Prenatal vitamin D₃ supplementation suppresses LL-37 peptide expression in ex vivo activated neonatal macrophages but not their killing capacity.

Raqib. Rubhana R; Ly. Anna A; Akhtar. Evana E; Mily. Akhirunnesa A; Perumal. Nandita N; Al-Mahmud. A...

Giving pregnant women a weekly dose of vitamin D lowered the amount of the antimicrobial peptide LL‑37 inside newborn immune cells when those cells were activated, but it didn’t change the cells' ability to kill bacteria in lab tests.

Utility 2
pubmed Jul 30, 2014

Transformation of human cathelicidin LL-37 into selective, stable, and potent antimicrobial compounds.

Wang. Guangshun G; Hanke. Mark L ML; Mishra. Biswajit B; Lushnikova. Tamara T; Heim. Cortney E CE; C...

Scientists tweaked the human antimicrobial peptide LL-37 to make it tougher against digestive enzymes and broaden its killing power against a wide range of dangerous bacteria. The new version, called 17BIPHE2, can break bacterial membranes, bind DNA, stop biofilm formation on catheters in mice, and even boost the body's own immune response. However, it’s still only tested in labs and mice, so it isn’t ready for personal use yet.

Utility 2
pubmed Jul 3, 2013

Acceleration of bone repair in NOD/SCID mice by human monoosteophils, novel LL-37-activated monocytes.

Zhang. Zhifang Z; Shively. John E JE

Scientists found that the natural peptide LL-37 can turn regular immune cells (monocytes) into a new type of bone‑forming cell called monoosteophils. When these cells were put into bone holes in special mice, the bones healed faster—about two weeks instead of three or more. The effect depends on a protein called MAPK13, and the cells show high levels of bone‑related genes.

Utility 2
pubmed Aug 15, 2014

NAD-dependent ADP-ribosylation of the human antimicrobial and immune-modulatory peptide LL-37 by ADP-ribosyltransferase-1.

Picchianti. Monica M; Russo. Carla C; Castagnini. Marta M; Biagini. Massimiliano M; Soldaini. Elisab...

Scientists found that the immune peptide LL-37 can have up to four of its five arginine spots chemically tagged with ADP‑ribose when it meets the enzyme ART1 and lots of NAD. This tagging adds negative charge, making LL-37 less positively charged, which could weaken its ability to stick to cell membranes and other negatively charged molecules like DNA. The change might alter how LL-37 works in the body, but the experiments were done in a test tube, not in people.

Utility 2
pubmed Jun 4, 2013

Neutrophils LL-37 migrate to the nucleus during overwhelming infection.

Pinheiro da Silva. Fabiano F; Medeiros. Maria Cristina Rodrigues MC; Dos Santos. Ângela Batista...

Scientists found that the immune peptide LL‑37, which normally fights germs outside cells, can actually move into the cell nucleus when the body is fighting a huge infection. This suggests LL‑37 might do more than just kill bacteria, possibly influencing how genes are turned on or off, but we don’t yet know what that means for health or performance.

Utility 2
pubmed Sep 27, 2014

Lack of cathelicidin processing in Papillon-Lefèvre syndrome patients reveals essential role of LL-37 in periodontal homeostasis.

Eick. Sigrun S; Puklo. Magdalena M; Adamowicz. Karina K; Kantyka. Tomasz T; Hiemstra. Pieter P; Sten...

The study shows that people with Papillon‑Lefèvre syndrome can't turn the protein hCAP18 into the antimicrobial peptide LL‑37 because a key enzyme is broken. Without LL‑37, harmful bacteria build up in the gums, causing severe early‑onset gum disease. This highlights LL‑37’s crucial role in keeping the mouth healthy.

Utility 2
pubmed Oct 29, 2013

Recombinant expression of novel protegrin-1 dimer and LL-37-linker-histatin-5 hybrid peptide mediated biotin carboxyl carrier protein fusion partner.

Orrapin. Santhasiri S; Intorasoot. Sorasak S

Scientists engineered bacteria to make two new antimicrobial peptides—a dimer of porcine protegrin‑1 and a hybrid of human LL‑37 linked to histatin‑5—then purified them and proved they kill E. coli and Staph aureus in lab tests. The work shows a way to produce these peptides, but it doesn’t give dosing, safety, or direct human‑use instructions.

Utility 2
pubmed Jan 9, 2013

Physiological relevance of LL-37 induced bladder inflammation and mast cells.

Oottamasathien. Siam S; Jia. Wanjian W; Roundy. Lindsi McCoard LM; Zhang. Jianxing J; Wang. Li L; Ye...

The study shows that the antimicrobial peptide LL-37 is found at very high levels in the urine of children with spina bifida and that, when put into mouse bladders, it causes inflammation that gets worse with higher doses and involves mast cells. This suggests that too much LL-37 can irritate the bladder and trigger immune cells.

Utility 2
pubmed Jul 15, 2013

Effect of intracellular expression of antimicrobial peptide LL-37 on growth of escherichia coli strain TOP10 under aerobic and anaerobic conditions.

Liu. Wei W; Dong. Shi Lei SL; Xu. Fei F; Wang. Xue Qin XQ; Withers. T Ryan TR; Yu. Hongwei D HD; Wan...

Scientists made E. coli produce the human antimicrobial peptide LL‑37 inside the cells and found it stops the bacteria from growing, both with oxygen and without. The peptide creates harmful reactive oxygen species when oxygen is present and makes the bacterial membrane leaky, while also messing with the bacteria’s energy‑making genes.

Utility 2
pubmed Jun 13, 2013

Cathelicidin LL-37 induces angiogenesis via PGE2-EP3 signaling in endothelial cells, in vivo inhibition by aspirin.

Salvado. M Dolores MD; Di Gennaro. Antonio A; Lindbom. Lennart L; Agerberth. Birgitta B; Haeggstr&#x...

The study shows that the human peptide LL‑37 can make blood‑vessel cells grow new vessels by turning on a chain of chemicals (COX‑1 → PGE2 → EP3). This effect can be stopped by aspirin, which blocks the same pathway. The findings are mostly basic science and don’t give dosage or safety info for people who might want to use LL‑37 as a supplement.

Utility 2
pubmed Feb 5, 2013

The human antimicrobial peptide LL-37, but not the mouse ortholog, mCRAMP, can stimulate signaling by poly(I:C) through a FPRL1-dependent pathway.

Singh. Divyendu D; Qi. Rongsu R; Jordan. Jarrat L JL; San Mateo. Lani L; Kao. C Cheng CC

The human peptide LL‑37 can grab double‑stranded RNA (like viral genetic material) and help it trigger immune sensors inside cells, while the mouse version can’t do this. This effect needs a specific cell‑surface receptor (FPRL1) and changes how the RNA is trafficked inside the cell.

Utility 2
pubmed Apr 11, 2013

Histone deacetylase inhibitors up-regulate LL-37 expression independent of toll-like receptor mediated signalling in airway epithelial cells.

Liu. Quan Q; Liu. Juan J; Roschmann. Kristina Irene Lisolette KIL; van Egmond. Danielle D; Golebski....

Researchers found that chemicals that block histone deacetylases, like the drug trichostatin A and the natural compound sodium butyrate, can turn on the gene for the antimicrobial peptide LL‑37 in airway cells. This effect happens even without viral‑mimic stimulation, and the same chemicals also dampen an inflammation signal (IL‑6). However, only the lab‑grown cell line showed more LL‑37 protein, not the primary nasal cells, so it’s still early evidence.

Utility 2
pubmed Jun 17, 2013

Human colonic mucus is a reservoir for antimicrobial peptides.

Antoni. Lena L; Nuding. Sabine S; Weller. Dagmar D; Gersemann. Michael M; Ott. German G; Wehkamp. Ja...

The study shows that the colon’s mucus layer naturally stores antimicrobial peptides like LL‑37 and still kills bacteria even when attached to mucus, meaning the gut’s own defenses stay active. This suggests that keeping the mucus barrier healthy could be important for gut immunity, but the paper doesn’t give a new supplement or dosage plan.

Utility 2
pubmed Oct 3, 2013

Role of the Vibrio cholerae matrix protein Bap1 in cross-resistance to antimicrobial peptides.

Duperthuy. Marylise M; Sjöström. Annika E AE; Sabharwal. Dharmesh D; Damghani. Fatemeh F;...

The study found that the cholera bacterium can release tiny vesicles that contain a protein called Bap1, which grabs onto the human antimicrobial peptide LL‑37 and blocks its action, giving the bacteria protection against both LL‑37 and another antibiotic called polymyxin B. For biohackers, this means that some bacteria can neutralize LL‑37, so its effectiveness may be limited in infections where Bap1‑producing microbes are present.

Utility 2
pubmed Aug 31, 2013

Cathelicidins: peptides with antimicrobial, immunomodulatory, anti-inflammatory, angiogenic, anticancer and procancer activities.

Wong. Jack Ho JH; Ye. Xiu Juan XJ; Ng. Tzi Bun TB

LL-37 is a natural protein your body makes that can kill microbes, tweak the immune system, reduce inflammation, affect blood vessel growth, and even influence cancer cells, both positively and negatively. The paper is a broad review, so it doesn’t give specific dosing or protocols for DIY use.