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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 3
pubmed Nov 28, 2009

Vitamin D(3) induces expression of human cathelicidin antimicrobial peptide 18 in newborns.

Misawa. Yuka Y; Baba. Atsushi A; Ito. Susumu S; Tanaka. Miyuki M; Shiohara. Masaaki M

The study shows that newborns have lower levels of the immune‑boosting peptide LL‑37 in their white blood cells compared to adults, but taking a form of vitamin D (1α‑hydroxy vitamin D3) for a month can raise LL‑37 levels in these cells. This suggests vitamin D can help strengthen the innate immune system, especially in people with low vitamin D or in early life.

Utility 3
pubmed Feb 26, 2010

Flagellin-induced corneal antimicrobial peptide production and wound repair involve a novel NF-kappaB-independent and EGFR-dependent pathway.

Gao. Nan N; Kumar. Ashok A; Jyot. Jeevan J; Yu. Fu-Shin FS

The study shows that a modified version of the bacterial protein flagellin can boost the body’s natural antimicrobial peptide LL‑37 and help heal corneal wounds without triggering the usual inflammatory response, meaning you could get protective benefits without side‑effects like swelling.

Utility 3
pubmed Jun 20, 2011

Induction of triggering receptor expressed on myeloid cells (TREM-1) in airway epithelial cells by 1,25(OH)₂ vitamin D₃.

Rigo. Isaura I; McMahon. Laura L; Dhawan. Puneet P; Christakos. Sylvia S; Yim. Sunghan S; Ryan. Lisa...

The study shows that taking the active form of vitamin D can turn on a receptor called TREM‑1 in airway cells, which then boosts the production of antimicrobial proteins like LL‑37 and beta‑defensin‑2, helping the lungs fight infections.

Utility 3
pubmed Jun 10, 2010

Antibiotic-induced Porphyromonas gingivalis LPS release and inhibition of LPS-stimulated cytokines by antimicrobial peptides.

Walters. S M SM; Dubey. V S VS; Jeffrey. N R NR; Dixon. D R DR

The study shows that antibiotics can cause the gum‑bacteria Porphyromonas gingivalis to release more harmful LPS, which triggers inflammation. The natural antimicrobial peptide LL‑37 was the best at neutralizing this LPS and stopping inflammatory cytokines in lab tests. This suggests that adding LL‑37‑like agents could help reduce inflammation when taking antibiotics for gum issues, though such peptides aren’t yet common as supplements.

Utility 3
pubmed Apr 19, 2010

LPS interactions with immobilized and soluble antimicrobial peptides.

Gustafsson. Anna A; Olin. Anders I AI; Ljunggren. Lennart L

Researchers tested short pieces of the natural peptide LL‑37 and similar molecules to see if they can grab and neutralize the harmful bacterial toxin LPS, both when floating in solution and when stuck onto a solid surface. They found that attaching the peptides to a filter doesn’t stop them from binding LPS, and the LL‑37‑derived and CEME‑derived peptides worked best at lowering the inflammatory signals that LPS normally triggers.

Utility 3
pubmed Apr 18, 2011

Pleiotropic regulation of macrophage polarization and tumorigenesis by formyl peptide receptor-2.

Li. Y Y; Cai. L L; Wang. H H; Wu. P P; Gu. W W; Chen. Y Y; Hao. H H; Tang. K K; Yi. P P; Liu. M M; M...

The study shows that the antimicrobial peptide LL‑37 can make liver cancer cells release signals (M‑CSF and MCP‑1) that push immune cells (macrophages) into a type that actually helps tumors grow. This effect works through a receptor called FPR2 and leads to more aggressive cancer behavior in lab and mouse experiments.

Utility 3
pubmed Jun 30, 2010

C-terminal peptides of tissue factor pathway inhibitor are novel host defense molecules.

Papareddy. Praveen P; Kalle. Martina M; Kasetty. Gopinath G; Mörgelin. Matthias M; Rydengå...

Researchers found that short pieces from the end of a protein called TFPI can kill a range of bacteria and fungi, acting like the well‑known antimicrobial peptide LL‑37. One piece, GGL27, works even better in normal blood because it triggers the complement system, and it also reduces harmful inflammation from bacterial toxins. TFPI is naturally present in skin and spikes up in wounds, suggesting it helps protect injured skin from infection.

Utility 3
pubmed 2010

The role of keratinocytes in defense against infection.

Schröder. Jens-Michael JM

This review explains how skin cells called keratinocytes use the antimicrobial peptide LL‑37 to keep the skin safe from germs. LL‑37 helps control skin cell death, and its production goes up after UV light exposure or signals from certain immune cells. When the system that makes LL‑37 is broken, as in some immune disorders, skin infections can happen.

Utility 3
pubmed Sep 21, 2009

Phenylbutyrate induces antimicrobial peptide expression.

Steinmann. Jonas J; Halldórsson. Skarphédinn S; Agerberth. Birgitta B; Gudmundsson. Gudmun...

The study shows that the drug phenylbutyrate (PBA) can boost the body's natural antimicrobial peptide LL‑37, especially when combined with vitamin D, by acting through specific cell signaling pathways. This suggests a possible way to strengthen immune defenses, but the compound is prescription‑only and its safety for long‑term use as a supplement isn’t established yet.

Utility 3
pubmed Jul 1, 2009

LL-37 complexation with glycosaminoglycans in cystic fibrosis lungs inhibits antimicrobial activity, which can be restored by hypertonic saline.

Bergsson. Gudmundur G; Reeves. Emer P EP; McNally. Paul P; Chotirmall. Sanjay H SH; Greene. Catherin...

The study found that in cystic fibrosis lungs, the natural antimicrobial peptide LL‑37 gets stuck to sugar‑like molecules (glycosaminoglycans), which blocks its ability to kill bacteria. Using hypertonic (salt‑rich) saline or enzymes that cut those sugar chains frees LL‑37, restoring its antibacterial power. This suggests that salty inhalations could boost innate immunity, especially if paired with agents that protect LL‑37 from being broken down.

Utility 3
pubmed Apr 26, 2008

NMR structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecylphosphocholine micelles.

Porcelli. Fernando F; Verardi. Raffaello R; Shi. Lei L; Henzler-Wildman. Katherine A KA; Ramamoorthy...

The study shows that the human antimicrobial peptide LL‑37 folds into two linked helices when it sits on membrane‑like surfaces, with the ends floppy and the middle part tightly packed. It lies flat on the membrane, exposing its water‑loving side while burying the oily side, supporting a “carpet” style of killing cells rather than punching holes. This structural insight helps explain how LL‑37 works and can guide the design of better versions or delivery methods.

Utility 3
pubmed Jul 26, 2008

PU.1 and bacterial metabolites regulate the human gene CAMP encoding antimicrobial peptide LL-37 in colon epithelial cells.

Termén. Stefan S; Tollin. Maria M; Rodriguez. Eduardo E; Sveinsdóttir. Sigrún H SH; J...

Researchers found that a gut‑derived molecule called butyrate, and another called lithocholic acid, can turn up the production of the antimicrobial peptide LL‑37 in colon cells. This boost is controlled by a protein called PU.1. While the work was done in a lab cell line, it hints that boosting butyrate through diet or supplements might help strengthen gut defenses, though the role of lithocholic acid is less clear and may carry risks.

Utility 3
pubmed Sep 3, 2009

Bactericidal activities of the cationic steroid CSA-13 and the cathelicidin peptide LL-37 against Helicobacter pylori in simulated gastric juice.

Leszczyńska. Katarzyna K; Namiot. Andrzej A; Fein. David E DE; Wen. Qi Q; Namiot. Zbigniew Z;...

The study shows that the natural peptide LL‑37, even though it’s higher in people with H. pylori infection, doesn’t kill the bacteria well in the stomach’s acidic, enzyme‑rich environment. A stronger lab‑made version, WLBU2, also loses its power in simulated stomach juice. In contrast, the synthetic compound CSA‑13 stays effective in low pH, survives pepsin, and isn’t blocked by stomach mucus, suggesting it could be a better candidate for treating H. pylori, especially resistant strains.

Utility 3
pubmed Jan 1, 2009

Effects of an LL-37-derived antimicrobial peptide in an animal model of biofilm Pseudomonas sinusitis.

Chennupati. Sri Kiran SK; Chiu. Alexander G AG; Tamashiro. Edwin E; Banks. Caroline A CA; Cohen. Mic...

In a rabbit study, a short version of the natural protein LL‑37 could wipe out Pseudomonas biofilms in the sinuses, but the doses that worked also irritated the tissue and damaged the tiny hair‑like cilia that keep the nose clean. Lower doses didn’t clear the infection well, and a standard antibiotic (tobramycin) worked similarly without the tissue damage.

Utility 3
pubmed 2009

Structure-function relationship of the human antimicrobial peptide LL-37 and LL-37 fragments in the modulation of TLR responses.

Molhoek. E Margo EM; den Hertog. Alice L AL; de Vries. Anne-Marij B C AM; Nazmi. Kamran K; Veerman....

The study shows that the human peptide LL‑37 can strongly block inflammation caused by certain bacterial signals (TLR4 and TLR2/1) while leaving other immune pathways untouched. The middle part of the peptide (amino acids 13‑31) does most of the work, and its ability to bind bacterial lipopolysaccharide depends on its positive charge and water‑repelling (hydrophobic) nature.

Utility 3
pubmed 2009

The roles of cathelicidin LL-37 in immune defences and novel clinical applications.

Nijnik. Anastasia A; Hancock. Robert E W RE

LL-37 is a natural antimicrobial peptide our bodies make that helps kill germs, guide immune cells, and heal wounds. Its production goes up when you have enough vitamin D3 or are in low‑oxygen conditions, and scientists are tweaking it to create new immune‑boosting drugs, but those are still experimental.

Utility 3
pubmed Nov 24, 2008

Evaluation of strategies for improving proteolytic resistance of antimicrobial peptides by using variants of EFK17, an internal segment of LL-37.

Strömstedt. Adam A AA; Pasupuleti. Mukesh M; Schmidtchen. Artur A; Malmsten. Martin M

Researchers tweaked a short piece of the human antimicrobial peptide LL‑37 (called EFK17) to make it tougher against body enzymes and better at killing bacteria. Swapping a few spots for the amino acid tryptophan (W) and adding end‑caps (amidation/acetylation) made the peptide resist breakdown by several key proteases and actually improved its antibacterial power, while keeping side‑effects low. Using all‑D‑amino acids stopped digestion completely but also made the peptide much weaker against microbes.

Utility 3
pubmed 2008

Analysis of neutrophil-derived antimicrobial peptides in gingival crevicular fluid suggests importance of cathelicidin LL-37 in the innate immune response against periodontogenic bacteria.

Puklo. M M; Guentsch. A A; Hiemstra. P S PS; Eick. S S; Potempa. J J

The study shows that a natural antimicrobial protein called LL‑37 is linked to gum disease. In people with chronic periodontitis, LL‑37 levels are higher but still may be broken down by harmful bacteria, which could weaken the mouth’s defense. This suggests that keeping LL‑37 levels up might help protect gums, but the research is observational and doesn’t test any treatments yet.

Utility 3
pubmed Sep 17, 2009

Vitamin D3 induces autophagy in human monocytes/macrophages via cathelicidin.

Yuk. Jae-Min JM; Shin. Dong-Min DM; Lee. Hye-Mi HM; Yang. Chul-Su CS; Jin. Hyo Sun HS; Kim. Kwang-Ky...

Vitamin D3 (the active form 1,25‑dihydroxyvitamin D3) makes immune cells produce the antimicrobial peptide LL‑37, and this peptide then turns on the cell's recycling system called autophagy, which helps destroy hidden bacteria like TB. The study shows the chain: vitamin D3 → LL‑37 → autophagy genes → better bacterial killing, all in lab‑grown human immune cells.