An antimicrobial peptide of the cathelicidin family that provides innate immune defense by killing pathogens and modulating inflammation and wound healing.
Scott. Monisha G MG; Davidson. Donald J DJ; Gold. Michael R MR; Bowdish. Dawn D; Hancock. Robert E W...
LL-37 is a natural human peptide that can calm down harmful inflammation caused by bacterial toxins while still calling immune cells to the infection site. In mice it stopped deadly shock from endotoxins and boosted helpful signaling molecules without raising classic inflammatory cytokines like TNF‑alpha. The work shows LL-37’s dual role as an anti‑sepsis agent and immune recruiter, but it’s still early‑stage and only tested in animals.
Dorschner. Robert A RA; Lopez-Garcia. Belen B; Massie. Jennifer J; Kim. Choll C; Gallo. Richard L RL
The study found that nails naturally contain a protein called LL‑37, which can kill the fungus Candida albicans, helping protect nails from infection even though they don’t have much immune cell activity.
Howell. Michael D MD; Jones. James F JF; Kisich. Kevin O KO; Streib. Joanne E JE; Gallo. Richard L R...
The study shows that the natural skin peptide LL‑37 (and its mouse version) can directly block vaccinia virus, the virus used in small‑pox vaccines, by stopping it from forming plaques, lowering its gene activity, and damaging its structure. Mice that lack this peptide get more skin lesions, suggesting the peptide helps protect against infection, especially in people with eczema who have low LL‑37 levels.
Henzler Wildman. Katherine A KA; Lee. Dong-Kuk DK; Ramamoorthy. A A
The study shows that the human peptide LL‑37 attacks cell membranes by lying flat on the surface and creating toroidal pores that bend the membrane, rather than punching through like a barrel or acting like a detergent. Its activity changes with the type of lipids and cholesterol present, but it doesn’t break membranes into tiny fragments.
Schauber. J J; Svanholm. C C; Termén. S S; Iffland. K K; Menzel. T T; Scheppach. W W; Melcher....
The study shows that short‑chain fatty acids (like butyrate, propionate and isobutyrate) boost the gut’s natural antimicrobial peptide LL‑37 in colon cells, and this boost is linked to cell maturation. Different signaling pathways control LL‑37 production and cell differentiation, meaning you can raise LL‑37 without necessarily changing how the cells mature.
Heilborn. Johan D JD; Nilsson. Margareta Frohm MF; Kratz. Gunnar G; Weber. Günther G; Søre...
The study shows that the natural peptide LL‑37 spikes after a skin cut, helps skin cells grow back, and is missing in stubborn chronic wounds. Blocking LL‑37 stops the skin from healing in lab tests, suggesting the peptide is important for wound closure.
Zaiou. Mohamed M; Nizet. Victor V; Gallo. Richard L RL
The study shows that the front part of the human antimicrobial peptide LL‑37, called the cathelin‑like domain, can both block a tissue‑damaging enzyme (cathepsin L) and kill harmful bacteria like E. coli and MRSA at micromolar levels, while the full‑length protein doesn’t do this on its own. This suggests the two halves of the molecule work together to protect skin.
Niyonsaba. F F; Someya. A A; Hirata. M M; Ogawa. H H; Nagaoka. I I
The study shows that the human peptide LL‑37 (and a similar peptide hBD‑2) can make mast cells release histamine and trigger inflammation signals, acting through calcium and G‑protein pathways. This suggests that taking LL‑37 could provoke allergic‑type reactions or affect inflammation, but the work was done in rat cells and doesn’t give dosing guidance for humans.
LL-37, a natural antimicrobial peptide, can kill certain oral bacteria at low concentrations, but its effect disappears when there’s a lot of salt or blood‑type proteins around. A slightly altered version, pentamide‑37, works a bit better in those conditions, hinting it could be a more useful drug in the future.
Hase. Koji K; Eckmann. Lars L; Leopard. John D JD; Varki. Nissi N; Kagnoff. Martin F MF
LL-37, an antimicrobial peptide, is mainly made by mature cells on the surface of the colon and goes up when those cells become more differentiated, especially after exposure to butyrate, a short‑chain fatty acid. It isn’t strongly triggered by common inflammatory signals or by most gut bacteria, though certain infections can raise it a bit.
In cystic fibrosis lungs, the natural antimicrobial peptide LL‑37 gets stuck in sticky bundles made of DNA and filamentous actin, which blocks its ability to kill bacteria. Enzymes or chemicals that break down DNA or actin (like the CF drug Dornase alfa, gelsolin, or polyaspartate) free LL‑37, letting it move into the fluid part of sputum where it can work. Bacterial LPS also ties up LL‑37, but a special LPS‑binding peptide can stop that interaction.
Wang. Y Y; Agerberth. B B; Löthgren. A A; Almstedt. A A; Johansson. J J
The study found that a common blood protein, apolipoprotein A‑I (apoA‑I), sticks to the human antimicrobial peptide LL‑37 and cuts its ability to kill bacteria in half when both are at the same level. This binding happens in normal plasma, not because the peptide is broken down, and blocking apoA‑I with antibodies restores LL‑37’s activity. For people experimenting with LL‑37 as a supplement or therapy, the results suggest that the peptide’s effectiveness could be limited when it circulates in the blood.
Johansson. J J; Gudmundsson. G H GH; Rottenberg. M E ME; Berndt. K D KD; Agerberth. B B
LL-37 is a human antimicrobial peptide that changes shape depending on its surroundings. It folds into a helix (the active form) when certain anions are present or when its concentration is high, and this shape makes it good at killing bacteria. However, very acidic conditions undo the helix, and in the body’s fluids the peptide can also harm human cells unless serum proteins block it.
LL-37 is the only cathelicidin peptide humans make, and it not only kills microbes but also helps control inflammation, cell growth, wound healing, and blood‑vessel formation. Scientists see it as a template for new drugs that could treat infections or tweak the immune system, but the paper is a review, not a new trial, so it doesn’t give dosing or specific DIY protocols.
Sørensen. Ole E OE; Cowland. Jack B JB; Theilgaard-Mönch. Kim K; Liu. Lide L; Ganz. Tomas...
The study shows that two growth factors, IGF‑1 and TGF‑α, trigger skin cells to make more of the antimicrobial peptide LL‑37 and other defense proteins, helping wounds heal and strengthening the skin’s barrier. This links growth‑factor activity directly to the body’s natural antibiotic defenses.
Murakami. M M; Ohtake. T T; Dorschner. R A RA; Gallo. R L RL
The study shows that the antimicrobial peptide LL‑37, part of the body’s natural defense, is present in human saliva and that its mouse counterpart is made in salivary glands and mouth lining. This means our mouths already have a built‑in antibiotic that helps keep harmful microbes at bay.
Scientists figured out a way to make a version of the human antimicrobial peptide LL‑37 in bacteria, then cut it out to get a usable peptide that works just like the natural one against bacteria.
Raqib. Rubhana R; Sarker. Protim P; Bergman. Peter P; Ara. Gul G; Lindh. Monica M; Sack. David A DA;...
In a rabbit model of shigellosis, giving oral butyrate twice daily for three days boosted the gut's own antimicrobial peptide (the rabbit version of LL‑37 called CAP‑18). This led to less illness, lower inflammation, and fewer bacteria in the stool. The study suggests that butyrate can turn on a natural antibiotic in the colon and help clear Shigella infections.
Andersson. Emma E; Rydengård. Victoria V; Sonesson. Andreas A; Mörgelin. Matthias M; Bj&#x...
The study shows that short protein fragments that stick to heparin (a sugar‑rich molecule) also kill bacteria and fungi. By looking at the charge, shape, and common patterns of these fragments, researchers found that many naturally occurring proteins contain hidden antimicrobial tricks. This insight could help design new, tiny “bio‑hacks” that fight infections.
Howell. Michael D MD; Wollenberg. Andreas A; Gallo. Richard L RL; Flaig. Michael M; Streib. Joanne E...
The natural skin peptide LL‑37 can kill herpes simplex virus (HSV) and people with atopic dermatitis who have low LL‑37 are more likely to get severe HSV skin infections (eczema herpeticum). Higher blood IgE levels tend to go with lower LL‑37, so IgE might hint at who’s at risk.