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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 Sep 25, 2008

Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles.

Wang. Guangshun G

LL-37 is a natural human peptide that kills bacteria by slipping into their membranes, and its shape is a curved helix that sticks to negatively‑charged lipids. A short piece of it, called KR‑12 (the last 12 amino acids), still kills bacteria but doesn’t harm human cells, making it a promising template for new antibiotics.

Utility 3
pubmed Jun 30, 2008

Human host defense peptide LL-37 prevents bacterial biofilm formation.

Overhage. Joerg J; Campisano. Andrea A; Bains. Manjeet M; Torfs. Ellen C W EC; Rehm. Bernd H A BH; H...

The human peptide LL-37 can stop the sticky layers (biofilms) that bacteria like Pseudomonas form, and it does this at a very low dose that the body could naturally reach. It also weakens already‑formed biofilms and works by making bacteria less likely to stick together and by messing with their communication system.

Utility 3
pubmed 2010

Selective antimicrobial action is provided by phenol-soluble modulins derived from Staphylococcus epidermidis, a normal resident of the skin.

Cogen. Anna L AL; Yamasaki. Kenshi K; Sanchez. Katheryn M KM; Dorschner. Robert A RA; Lai. Yuping Y;...

Researchers found that two small proteins (PSMγ and PSMδ) made by a harmless skin bacterium act like the human peptide LL‑37: they form helix shapes, stick to cell membranes, and kill bad skin bugs such as Staph aureus while leaving the good bacteria unharmed. They also boost each other's and LL‑37’s antimicrobial power, especially against Group A Strep on mouse skin.

Utility 3
pubmed Apr 22, 2010

Changes of antimicrobial peptides and transepidermal water loss after topical application of tacrolimus and ceramide-dominant emollient in patients with atopic dermatitis.

Park. Kui Young KY; Kim. Dong Ha DH; Jeong. Mi Sook MS; Li. Kapsok K; Seo. Seong Jun SJ

In a tiny study of three eczema patients, applying either a prescription cream (tacrolimus) or a ceramide‑rich moisturizer to the skin for four weeks both raised levels of the antimicrobial peptide LL‑37 (and another peptide, hBD‑2) and lowered water loss through the skin. The two treatments worked about the same, showing that fixing the skin barrier also boosts the skin’s natural antimicrobial defense.

Utility 3
pubmed Sep 2, 2008

The human cathelicidin LL-37 modulates the activities of the P2X7 receptor in a structure-dependent manner.

Tomasinsig. Linda L; Pizzirani. Cinzia C; Skerlavaj. Barbara B; Pellegatti. Patrizia P; Gulinelli. S...

The study shows that the natural peptide LL‑37 can boost cell growth by activating a protein called P2X7, which normally responds to ATP released during injury. This effect depends on the peptide’s shape, not its handedness, and LL‑37 can make the P2X7 channel work stronger, even in a shortened version of the protein. The work was done in lab cells, not people.

Utility 3
pubmed Aug 31, 2008

The role of antimicrobial peptides in human skin and in skin infectious diseases.

Schittek. Birgit B; Paulmann. Maren M; Senyürek. Ilknur I; Steffen. Heiko H

LL-37 is a natural protein in our skin that helps kill germs and calm inflammation. People with eczema, burns or chronic wounds have less of it, while those with psoriasis or acne have more, which seems to protect them from infections. This suggests that boosting LL-37 on the skin could help prevent or treat infections and improve wound healing, but the exact way to do it isn’t worked out yet.

Utility 3
pubmed Jul 23, 2009

Injury downregulates the expression of the human cathelicidin protein hCAP18/LL-37 in atopic dermatitis.

Mallbris. Lotus L; Carlén. Lina L; Wei. Tianling T; Heilborn. Johan J; Nilsson. Margareta Frohm...

In eczema (atopic dermatitis), the skin’s natural antibiotic protein LL‑37 is normally low in rash areas and, unlike healthy skin, doesn’t rise after the skin is scratched or injured. However, vitamin D can still boost LL‑37 production even in these inflamed patches, meaning vitamin D helps keep the skin’s antimicrobial defense working despite eczema.

Utility 3
pubmed 2010

The role of salivary histatin and the human cathelicidin LL-37 in wound healing and innate immunity.

Oudhoff. Menno J MJ; Blaauboer. Marjolein E ME; Nazmi. Kamran K; Scheres. Nina N; Bolscher. Jan G M...

The study shows that the antimicrobial peptide LL‑37 can boost skin cell movement and growth, which helps wounds close faster, but only at a very specific low dose (about 1 µM). Higher amounts kill the cells. A related saliva peptide, Histatin‑2, also speeds cell movement without causing cell death or inflammation, but it doesn’t make cells multiply.

Utility 3
pubmed Jan 5, 2010

Staphylococcus epidermidis antimicrobial delta-toxin (phenol-soluble modulin-gamma) cooperates with host antimicrobial peptides to kill group A Streptococcus.

Cogen. Anna L AL; Yamasaki. Kenshi K; Muto. Jun J; Sanchez. Katheryn M KM; Crotty Alexander. Laura L...

The study shows that a small protein called delta-toxin, made by the harmless skin bacterium Staphylococcus epidermidis, works together with the body's own antimicrobial peptides (including LL‑37) to kill the harmful Group A Streptococcus bacteria. The peptide is naturally found on human skin, can boost neutrophil trap activity, and helps reduce bacterial survival in mouse wound models.

Utility 3
pubmed Sep 1, 2009

Structure dependence of biological activities for primate cathelicidins.

Tomasinsig. Linda L; Morgera. Francesca F; Antcheva. Nikolinka N; Pacor. Sabrina S; Skerlavaj. Barba...

The study shows that tiny changes in the shape and electric charge of LL‑37‑like peptides dramatically change how well they kill bacteria and how toxic they are to human cells. More positively charged, unstructured versions kill bacteria better and aren’t slowed down by salt or serum, but they can also be more harmful to our own cells, especially depending on the cell’s health. The human version, which folds into a helix, is less potent against microbes but still can be toxic under certain conditions.

Utility 3
pubmed Aug 8, 2009

Antimicrobial peptide inhibition of Porphyromonas gingivalis 381-induced hemagglutination is improved with a synthetic decapeptide.

Dixon. Douglas R DR; Jeffrey. Nicole R NR; Dubey. Vinod S VS; Leung. Kai P KP

The study shows that the natural antimicrobial peptide LL‑37 can block a key step (hemagglutination) that Porphyromonas gingivalis uses to stick to cells, and that a small lab‑made peptide called KSL‑W makes this blocking effect even stronger when used together. LL‑37 works best, histatin 5 is also good, and KSL‑W alone isn’t very strong but doesn’t cause unwanted blood‑cell clumping.

Utility 3
pubmed Jul 14, 2008

The commensal Streptococcus salivarius K12 downregulates the innate immune responses of human epithelial cells and promotes host-microbe homeostasis.

Cosseau. Celine C; Devine. Deirdre A DA; Dullaghan. Edie E; Gardy. Jennifer L JL; Chikatamarla. Avin...

The study shows that the probiotic bacterium Streptococcus salivarius K12 can calm down inflammation in airway cells by cutting down the release of IL‑8 and other signals, even when the cells are challenged with the antimicrobial peptide LL‑37 or harmful bacteria. It does this by dampening the NF‑kappaB pathway and tweaking many genes linked to cell health and barrier function.

Utility 3
pubmed Nov 1, 2006

Innate immune peptide LL-37 displays distinct expression pattern from beta-defensins in inflamed gingival tissue.

Hosokawa. I I; Hosokawa. Y Y; Komatsuzawa. H H; Goncalves. R B RB; Karimbux. N N; Napimoga. M H MH;...

The study shows that the antimicrobial peptide LL‑37 is especially made by immune cells in inflamed gums and its amount grows with the severity of gum disease, while gum lining cells always make it regardless of inflammation. This suggests LL‑37 plays a key role in oral immunity and could be a target for keeping gums healthy, which may affect overall inflammation and health.

Utility 3
pubmed Oct 7, 2006

Recombinant expression of human cathelicidin (hCAP18/LL-37) in Pichia pastoris.

Hong. In-Pyo IP; Lee. Sung-Jae SJ; Kim. Yong-Seok YS; Choi. Shin-Geon SG

Scientists showed they can make the human antimicrobial peptide LL‑37 inside a common yeast (Pichia pastoris) and pull it out with activity against bacteria. The peptide comes out a bit larger because it still has an extra methionine at the start. This proves the yeast system can be used to produce LL‑37 without fancy fusion tricks.

Utility 3
pubmed 2008

Efficacy of LL-37 and granulocyte colony-stimulating factor in a neutropenic murine sepsis due to Pseudomonas aeruginosa.

Cirioni. Oscar O; Ghiselli. Roberto R; Tomasinsig. Linda L; Orlando. Fiorenza F; Silvestri. Carmela...

In a mouse study, giving the natural antimicrobial peptide LL‑37 together with the immune‑boosting drug G‑CSF helped neutropenic mice survive a deadly Pseudomonas infection better than either treatment alone or standard antibiotics.

Utility 3
pubmed Sep 13, 2007

In vitro and in vivo wound healing-promoting activities of human cathelicidin LL-37.

Carretero. Marta M; Escámez. María J MJ; García. Marta M; Duarte. Blanca B; Holgu&#xe...

LL-37, a natural antimicrobial peptide, was shown to speed up skin cell movement and trigger several healing‑related signals in lab dishes, and when delivered via a virus to diabetic mice it helped wounds close faster and form better tissue. This suggests LL-37 could be useful for wound repair, but the study used gene‑therapy delivery and didn’t test creams or sprays that people could apply themselves.

Utility 3
pubmed Feb 15, 2007

A novel method for purifying recombinant human host defense cathelicidin LL-37 by utilizing its inherent property of aggregation.

Li. Yifeng Y; Li. Xia X; Li. He H; Lockridge. Oksana O; Wang. Guangshun G

Researchers have found a simpler way to make the immune‑boosting peptide LL‑37 in the lab. By letting the peptide naturally clump together, they can pull it out of the mixture more easily, cut it free with chemicals, and end up with about half again as much peptide as before, using fewer steps.

Utility 3
pubmed 2006

In silico identification and biological evaluation of antimicrobial peptides based on human cathelicidin LL-37.

Sigurdardottir. Thorgerdur T; Andersson. Pia P; Davoudi. Mina M; Malmsten. Martin M; Schmidtchen. Ar...

Researchers cut the human antimicrobial peptide LL-37 down to a 21‑amino‑acid piece called GKE, which still kills bacteria and neutralizes harmful LPS but is gentler on human cells, making it a promising lead for safer peptide‑based anti‑sepsis drugs.

Utility 3
pubmed 2006

Multifunctional roles of human cathelicidin (LL-37) at the ocular surface.

Huang. Ling C LC; Petkova. Tihomira D TD; Reins. Rose Y RY; Proske. Rita J RJ; McDermott. Alison M A...

LL-37 is a natural protein found in the eye’s surface that rises after a corneal injury, kills harmful bacteria even in salty tears, and helps eye cells move to close wounds, though it doesn’t make them multiply and can be toxic at high doses.