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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 Jun 13, 1997

The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders.

Frohm. M M; Agerberth. B B; Ahangari. G G; Stâhle-Bäckdahl. M M; Lidén. S S; Wigzell....

The study shows that the antimicrobial peptide LL‑37 is produced more in skin cells when the skin is inflamed, like in psoriasis, and helps fight bacteria. In healthy skin this peptide isn’t increased. This suggests LL‑37 is part of the body’s first‑line defense when the skin barrier is damaged.

Utility 2
pubmed Jun 14, 2007

ETCare: a randomized, controlled, masked trial comparing two solutions for upper airway care in the NICU.

Christensen. R D RD; Rigby. G G; Schmutz. N N; Lambert. D K DK; Wiedmeier. S E SE; Burnett. J J; Sco...

A new low‑salt solution called ETCare was tested in newborns on ventilators and was found to be just as well tolerated as regular saline. It may help keep the natural antimicrobial peptide LL‑37 active in the airway, which could lower infection risk, but the study was small and only showed trends, not definitive proof.

Utility 2
pubmed 2004

Proteus mirabilis ZapA metalloprotease degrades a broad spectrum of substrates, including antimicrobial peptides.

Belas. Robert R; Manos. Jim J; Suvanasuthi. Rooge R

The study shows that a bacterial enzyme called ZapA, made by the urinary‑tract bug Proteus mirabilis, can cut up the human antimicrobial peptide LL‑37, making it lose its ability to kill microbes. This means infections with this bacterium could neutralize any LL‑37 you might be taking or relying on for immune support.

Utility 2
pubmed Feb 1, 2003

Effects of human cathelicidin antimicrobial peptide LL-37 on lipopolysaccharide-induced nitric oxide release from rat aorta in vitro.

Ciornei. C D CD; Egesten. A A; Bodelsson. M M

The study shows that the human peptide LL‑37 can block some harmful effects of bacterial toxins (LPS) on blood vessels in rat tissue, lowering nitric‑oxide production and protecting vessel function, but high doses can damage cells. This is an early‑stage lab finding, not a human trial, so it’s mostly a safety and mechanism note for biohackers.

Utility 2
pubmed Jan 15, 2004

The cationic antimicrobial peptide LL-37 modulates dendritic cell differentiation and dendritic cell-induced T cell polarization.

Davidson. Donald J DJ; Currie. Andrew J AJ; Reid. Gregor S D GS; Bowdish. Dawn M E DM; MacDonald. Ke...

The study shows that the natural peptide LL‑37 can change how immune cells called dendritic cells develop, making them better at grabbing stuff, showing more activation signals, and pushing other immune cells toward a Th‑1 type response, which is important for fighting infections.

Utility 2
pubmed Jan 1, 2003

Antimicrobial peptide LL-37 is upregulated in chronic nasal inflammatory disease.

Kim. Seon Tae ST; Cha. Heung Eog HE; Kim. Dong Young DY; Han. Gyu Cheol GC; Chung. Yoo-Sam YS; Lee....

The study found that the natural antimicrobial peptide LL‑37 is more abundant in the noses of people with chronic sinus inflammation compared to healthy noses, and it shows up alongside other inflammation signals like IL‑1β and IL‑8.

Utility 2
pubmed Oct 28, 2008

APD2: the updated antimicrobial peptide database and its application in peptide design.

Wang. Guangshun G; Li. Xia X; Wang. Zhe Z

The updated APD2 database now holds over a thousand antimicrobial peptides and lets users filter by family, source, modifications, and targets. By looking at which amino acids appear most often in natural peptides, the researchers designed three new peptides, and one of them (GLK‑19) killed E. coli better than the human peptide LL‑37.

Utility 2
pubmed Dec 15, 2003

The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor.

Tjabringa. G Sandra GS; Aarbiou. Jamil J; Ninaber. Dennis K DK; Drijfhout. Jan Wouter JW; Søren...

LL-37, a natural peptide released by immune cells, not only kills microbes but also activates lung‑lining cells by turning on the EGFR‑driven signaling pathway, which leads to inflammation‑related signals like IL‑8.

Utility 2
pubmed 2003

An angiogenic role for the human peptide antibiotic LL-37/hCAP-18.

Koczulla. Rembert R; von Degenfeld. Georges G; Kupatt. Christian C; Krötz. Florian F; Zahler. S...

LL-37 is a natural peptide that not only fights microbes but also helps grow new blood vessels, which can speed up wound healing. In animal experiments, adding LL-37 boosted blood‑vessel formation, while mice missing the peptide healed more slowly, showing its role in tissue repair.

Utility 2
pubmed 2003

Expression of LL-37 by human gastric epithelial cells as a potential host defense mechanism against Helicobacter pylori.

Hase. Koji K; Murakami. Masamoto M; Iimura. Mitsutoshi M; Cole. Sheri P SP; Horibe. Yoshimune Y; Oht...

Your stomach lining makes a natural antimicrobial peptide called LL-37. When you have a Helicobacter pylori infection, the stomach cells crank up LL-37 production, and the peptide can directly kill the bacteria, especially when teamed up with another defense peptide. This shows LL-37 is part of the gut’s innate defense system.

Utility 2
pubmed 2002

Augmentation of the lipopolysaccharide-neutralizing activities of human cathelicidin CAP18/LL-37-derived antimicrobial peptides by replacement with hydrophobic and cationic amino acid residues.

Nagaoka. Isao I; Hirota. Satoko S; Niyonsaba. François F; Hirata. Michimasa M; Adachi. Yoshiyuk...

Scientists tweaked a natural human peptide called LL-37 to make it stick better to bacterial toxins (LPS) and calm the immune response. The best version, named 18‑mer LLKKK, bound LPS strongly, lowered inflammatory signals in cells, and saved mice from deadly toxin shock. However, this work is still early‑stage and only tested in lab dishes and mice, so it isn’t ready for personal use yet.

Utility 2
pubmed Jun 15, 2001

Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3.

Sørensen. O E OE; Follin. P P; Johnsen. A H AH; Calafat. J J; Tjabringa. G S GS; Hiemstra. P S...

The study shows that the human antimicrobial peptide LL‑37 is made when neutrophils release a larger protein (hCAP‑18) and an enzyme called proteinase 3 cuts it outside the cell. This cutting doesn’t happen inside the cell’s digestive compartments, only after the granules are expelled.

Utility 2
pubmed Sep 1, 2005

Human antimicrobial peptides: defensins, cathelicidins and histatins.

De Smet. Kris K; Contreras. Roland R

The article reviews three groups of human antimicrobial peptides—defensins, histatins, and the cathelicidin LL-37—explaining their basic structures and how they act against microbes. LL-37 is a small protein fragment that changes shape depending on its environment, becoming an alpha‑helix in oily conditions.

Utility 2
pubmed 2000

Activity of cecropin P1 and FA-LL-37 against urogenital microflora.

Smeianov. V V; Scott. K K; Reid. G G

The study shows two antimicrobial peptides, FA‑LL‑37 and cecropin P1, can kill common urinary‑tract bacteria like E. coli, P. aeruginosa and K. pneumoniae at micromolar levels while mostly leaving beneficial lactobacilli untouched, suggesting they might be useful in a topical cream for UTIs, but the work is still early and no human dosing or safety info is provided.

Utility 2
pubmed 1998

Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils.

Turner. J J; Cho. Y Y; Dinh. N N NN; Waring. A J AJ; Lehrer. R I RI

LL-37 is a natural protein from white blood cells that can kill a wide range of bacteria, including some antibiotic‑resistant strains, at fairly low doses. Its ability to break bacterial membranes and bind toxic bacterial components (LPS) suggests it helps protect skin and possibly lungs, especially in conditions like cystic fibrosis, but the study only tests it in lab dishes, not in people.

Utility 2
pubmed Mar 1, 2004

Polysaccharide intercellular adhesin (PIA) protects Staphylococcus epidermidis against major components of the human innate immune system.

Vuong. Cuong C; Voyich. Jovanka M JM; Fischer. Elizabeth R ER; Braughton. Kevin R KR; Whitney. Adeli...

The study shows that a sugar coating (PIA) on the skin bacteria Staphylococcus epidermidis helps it hide from the body’s natural defenses, including the antimicrobial peptide LL‑37. Without this coating, the bacteria are easier for immune cells and skin peptides to kill.

Utility 2
pubmed Jun 1, 1996

The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes.

Gudmundsson. G H GH; Agerberth. B B; Odeberg. J J; Bergman. T T; Olsson. B B; Salcedo. R R

Scientists mapped the human gene that makes the antimicrobial peptide LL‑37, showing it’s the only cathelicidin gene in our DNA and that it’s produced in white‑blood cells, likely controlled by inflammation signals like interleukin‑6.

Utility 2
pubmed Nov 29, 2004

Impact of LL-37 on anti-infective immunity.

Bowdish. Dawn M E DM; Davidson. Donald J DJ; Lau. Y Elaine YE; Lee. Ken K; Scott. Monisha G MG; Hanc...

LL-37 is a natural human peptide that rises at infection sites and can tweak the immune system, helping cells release signals and steering immune cells toward a stronger defense. Even when it doesn't kill germs directly, it can still protect animals from infections by boosting immunity.