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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 Jul 6, 2004

Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37.

Henzler-Wildman. Katherine A KA; Martinez. Gary V GV; Brown. Michael F MF; Ramamoorthy. A A

LL-37 is a human antimicrobial peptide that slips into the oily part of cell membranes, disturbing the packing of fat chains and helping to break the membrane. The study shows it goes about 5‑6 Å deep and that both its charge and its ability to fit into the membrane are important, with the effect changing depending on the type of lipids and temperature.

Utility 2
pubmed 2004

Expression of LL-37, human beta defensin-2, and CCR6 mRNA in patients with psoriasis vulgaris.

Li. Dongsheng D; Li. Jiawen J; Duan. Yiqun Y; Zhou. Xiaoyong X

The study found that people with psoriasis have higher levels of the antimicrobial peptides LL‑37 and hBD‑2, as well as more of the CCR6 receptor, in their skin lesions compared to normal skin. This may explain why psoriasis patients rarely get skin infections, but the research doesn’t tell you how to use or boost these peptides in everyday life.

Utility 2
pubmed 2005

The human cathelicidin LL-37: a multifunctional peptide involved in infection and inflammation in the lung.

Tjabringa. G Sandra GS; Rabe. Klaus F KF; Hiemstra. Pieter S PS

LL-37 is a natural peptide made by immune cells in the lungs that can kill a wide range of germs and also affect inflammation, cell movement, blood vessel growth, and wound healing. This review explains how these multiple actions could be useful when designing new antimicrobial treatments, but it doesn’t give specific dosing or usage tips.

Utility 2
pubmed Jun 30, 2007

The antimicrobial peptide LL-37 inhibits HIV-1 replication.

Bergman. Peter P; Walter-Jallow. Lilian L; Broliden. Kristina K; Agerberth. Birgitta B; Söderlu...

The human antimicrobial peptide LL-37 can stop HIV-1 from multiplying in immune cells in lab dishes. It works against several strains of the virus and doesn't need to change the usual HIV entry points on the cells. This suggests LL-37 might help protect tissues that naturally make it, like the lining of the mouth or gut.

Utility 2
pubmed 2004

Antibacterial activities of the cathelicidins prophenin (residues 62 to 79) and LL-37 in the presence of a lung surfactant preparation.

Wang. Yuqin Y; Walter. Gabi G; Herting. Egbert E; Agerberth. Birgitta B; Johansson. Jan J

The study shows that the natural antimicrobial peptide LL‑37 can kill certain lung‑related bacteria, but the lung’s own surfactant can dampen its effect unless you use a fairly high dose. A related peptide, PF‑18, is even more blocked by surfactant at low doses. At very high concentrations, both peptides work better and don’t mess up the surfactant’s surface properties.

Utility 2
pubmed Sep 22, 2005

Vernix caseosa as a multi-component defence system based on polypeptides, lipids and their interactions.

Tollin. M M; Bergsson. G G; Kai-Larsen. Y Y; Lengqvist. J J; Sjövall. J J; Griffiths. W W; Sk&#...

The study shows that the newborn’s skin coating, called vernix, contains the antimicrobial peptide LL‑37 along with other protective proteins, and that the fats in vernix make LL‑37 work better against microbes. This tells us that LL‑37’s activity can be boosted by certain lipids, but the research is limited to newborn skin and doesn’t give dosage or direct health‑boosting advice for adults.

Utility 2
pubmed May 15, 2005

Mouse cathelin-related antimicrobial peptide chemoattracts leukocytes using formyl peptide receptor-like 1/mouse formyl peptide receptor-like 2 as the receptor and acts as an immune adjuvant.

Kurosaka. Kahori K; Chen. Qian Q; Yarovinsky. Felix F; Oppenheim. Joost J JJ; Yang. De D

The mouse version of the human antimicrobial peptide LL‑37 (called CRAMP) can pull immune cells to where it’s needed and boost the body’s response to a vaccine‑like challenge, working through a specific cell‑surface receptor. This shows that LL‑37 isn’t just an antimicrobial; it also helps direct immune cells and can act as an immune‑enhancing agent in mice.

Utility 2
pubmed Dec 9, 2004

Interactions between neutrophil-derived antimicrobial peptides and airway epithelial cells.

van Wetering. Sandra S; Tjabringa. G Sandra GS; Hiemstra. Pieter S PS

LL-37, a natural peptide made by white blood cells, can talk to the cells lining your airways. It can boost the release of signaling molecules, attract other immune cells, and help those airway cells grow and heal. The paper reviews these effects but doesn’t give dosing tips or new ways to use the peptide for health hacks.

Utility 2
pubmed Mar 1, 2004

Innate immunity and mucosal bacterial interactions in the intestine.

Eckmann. Lars L

This review explains how the gut’s built‑in immune system spots and fights bacteria, highlighting the role of the peptide LL‑37 (the only human cathelicidin) as a broad‑spectrum antimicrobial that also helps regulate inflammation and blood vessel growth. It also covers other sensors like Toll‑like receptors and NOD proteins, and notes that problems with NOD2 are linked to Crohn’s disease.

Utility 2
pubmed Apr 3, 2006

In situ characterization of lipid A interaction with antimicrobial peptides using surface X-ray scattering.

Neville. Frances F; Hodges. Chris S CS; Liu. Chao C; Konovalov. Oleg O; Gidalevitz. David D

The study shows that the human antimicrobial peptide LL‑37 can slip into a model of the outer membrane component (lipid A) of Gram‑negative bacteria, but it doesn’t dramatically change the membrane’s structure, suggesting the peptide’s effect is subtle and the lipid tails stay fairly rigid.

Utility 2
pubmed 2005

Antimicrobial peptides in lung inflammation.

Beisswenger. Christoph C; Bals. Robert R

LL‑37 is a natural protein made by many cells in the lungs that not only kills germs directly but also talks to other immune cells to shape inflammation. Its levels go up or down in different lung diseases, showing it plays a key role in lung health.

Utility 2
pubmed Jun 20, 2005

Induced resistance to the antimicrobial peptide lactoferricin B in Staphylococcus aureus.

Samuelsen. Orjan O; Haukland. Hanne H HH; Jenssen. Håvard H; Krämer. Manuela M; Sandvik. K...

The study found that Staph bacteria can become resistant to the antimicrobial peptide lactoferricin B when repeatedly exposed, but this resistance fades when the peptide is removed and the bacteria do not become resistant to the human peptide LL‑37.

Utility 2
pubmed Jun 1, 2005

The antimicrobial peptide rCRAMP is present in the central nervous system of the rat.

Bergman. Peter P; Termén. Stefan S; Johansson. Linda L; Nyström. Lisbeth L; Arenas. Ernest...

Scientists discovered that rats make a natural antimicrobial peptide called rCRAMP (similar to human LL‑37) inside the brain, especially in areas like the olfactory bulb, cerebellum, medulla and spinal cord, and that this peptide can kill bacteria in lab tests, hinting it helps protect the brain from infection.

Utility 2
pubmed Mar 1, 2005

Defence molecules in intestinal innate immunity against bacterial infections.

Eckmann. Lars L

The review explains that LL-37 is a natural protein made by gut lining cells, neutrophils and mast cells, and besides killing bacteria it can help grow new blood vessels, attract immune cells and trigger signaling molecules. It’s part of a larger family of antimicrobial peptides that each work in different parts of the intestine.

Utility 2
pubmed 2006

Cytokine milieu of atopic dermatitis skin subverts the innate immune response to vaccinia virus.

Howell. Michael D MD; Gallo. Richard L RL; Boguniewicz. Mark M; Jones. James F JF; Wong. Cathy C; St...

The study shows that the skin peptide LL‑37 helps stop vaccinia virus, but in eczema‑type skin (atopic dermatitis) the immune signals IL‑4 and IL‑13 lower LL‑37, letting the virus grow more. Blocking those signals or adding LL‑37 restores the skin’s ability to fight the virus.

Utility 2
pubmed 2006

Inhibition of antimicrobial peptides by group A streptococci: SIC and DRS.

Fernie-King. B A BA; Seilly. D J DJ; Lachmann. P J PJ

Some especially nasty group A strep bacteria make proteins (SIC and DRS) that can neutralize LL‑37, a natural antimicrobial peptide your body uses to fight infections, along with several other immune proteins. This means that during a strep infection, the bacteria can blunt part of your innate defense.

Utility 2
pubmed Apr 9, 2005

Host defense effector molecules in mucosal secretions.

Tjabringa. G Sandra GS; Vos. Joost B JB; Olthuis. Diana D; Ninaber. Dennis K DK; Rabe. Klaus F KF; S...

The study measured the natural levels of the antimicrobial peptide LL‑37 and other protective proteins in different body fluids, finding that semen has especially high amounts of LL‑37 and related inhibitors, while each fluid has its own unique mix. This tells us where the body naturally concentrates this peptide but doesn’t give a new way to use it.

Utility 2
pubmed Feb 23, 2010

Differential activity of innate defense antimicrobial peptides against Nocardia species.

Rieg. Siegbert S; Meier. Benjamin B; Fähnrich. Eva E; Huth. Anja A; Wagner. Dirk D; Kern. Winfr...

The study shows that the antibacterial peptide LL-37 and other natural defense proteins can kill some Nocardia bacteria, but their effectiveness depends on the exact species. Human neutrophil peptides (HNP‑1‑3) and a bovine peptide called indolicidin work best across several strains, while LL‑37 is less consistently effective.

Utility 2
pubmed Oct 2, 2000

LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells.

Chen. Q Q; Schmidt. A P AP; Anderson. G M GM; Wang. J M JM; Wooters. J J; Oppenheim. J J JJ; Chertov...

LL-37, a natural peptide made by white blood cells and skin cells, can attract other immune cells like neutrophils, monocytes, and T‑cells by binding to a receptor called FPRL1, and it triggers calcium signals inside those cells.

Utility 2
pubmed Feb 22, 2005

Expression of an additional cathelicidin antimicrobial peptide protects against bacterial skin infection.

Lee. Phillip H A PH; Ohtake. Takaaki T; Zaiou. Mohamed M; Murakami. Masamoto M; Rudisill. Jennifer A...

Adding a second cathelicidin peptide (PR‑39) to the human peptide LL‑37 makes skin cells better at killing group A strep in lab tests, and mice engineered to constantly produce PR‑39 get smaller infections. The study shows the concept works in animals, but it doesn’t give a human‑ready recipe or safety data.