An antimicrobial peptide of the cathelicidin family that provides innate immune defense by killing pathogens and modulating inflammation and wound healing.
Wan. Min M; Soehnlein. Oliver O; Tang. Xiao X; van der Does. Anne M AM; Smedler. Erik E; Uhlén....
The study shows that the natural peptide LL-37 can trigger immune cells (macrophages) to release inflammation‑related molecules called eicosanoids (LTB4 and TXA2) in two waves: an early burst that depends on calcium signaling, and a later burst that comes from increased COX‑2 enzyme activity. This effect was seen in human cells in a dish and also in mice, suggesting LL-37 helps control the timing of inflammatory responses.
When eye cells called MĂĽller glia encounter Staph bacteria, they ramp up production of the antimicrobial peptide LL-37 (along with other defensins), release reactive oxygen and nitrogen species, and can actually engulf and kill the bacteria, acting like immune cells.
Scheb-Wetzel. Matthias M; Rohde. Manfred M; Bravo. Alicia A; Goldmann. Oliver O
Researchers found that mouse mast cells can kill the tough gut bug Enterococcus faecalis by releasing a natural antimicrobial peptide called LL‑37 and by throwing out web‑like traps. This killing needs certain immune sensors (TLR2 and MyD88). The work shows LL‑37 is a powerful weapon against this resistant bacterium, but it’s an early‑stage lab finding, not a ready‑to‑use supplement protocol.
Sørensen. Ole E OE; Clemmensen. Stine N SN; Dahl. Sara L SL; Østergaard. Ole O; Heegaard....
The study shows that a genetic defect that blocks the enzyme cathepsin C stops the body from turning the precursor protein hCAP‑18 into the antimicrobial peptide LL‑37, and also wipes out several key neutrophil enzymes. Even without these enzymes, the patient didn’t have major infections, suggesting the body can cope without them. This tells us that LL‑37 production relies on specific enzymes, and that simply having neutrophils isn’t enough if those enzymes are missing.
Nuding. Sabine S; Frasch. Tina T; Schaller. Martin M; Stange. Eduard F EF; Zabel. Lutz T LT
The study found that the human antimicrobial peptide LL‑37 works together with several antibiotics to kill the gut bug Clostridium difficile more effectively in lab tests, mainly by messing up the bacteria’s outer layer so the drugs get in better. However, the peptide isn’t something you can buy as a supplement, and in a few toxin‑producing strains it actually caused more toxin to be released.
Burchacka. Ewa E; Sieńczyk. Marcin M; Frick. Inga-Maria IM; Wysocka. Magdalena M; Lesner. Adam...
The bacteria Finegoldia magna makes an enzyme called SufA that can cut up the human antimicrobial peptide LL‑37 and also break down fibrinogen, which may help the bacteria spread. Researchers mapped which protein pieces SufA likes to cut and found a chemical (Cbz‑6‑AmNphth(P)(OPh)2) that can block the enzyme. This blocker stopped SufA from destroying fibrinogen in lab tests and also killed several bacteria, including F. magna, Staph aureus and E. coli.
Falcao. C B CB; de La Torre. B G BG; Pérez-Peinado. C C; Barron. A E AE; Andreu. D D; Rádi...
Scientists discovered four new snake‑venom peptides called vipericidins that act like the human antimicrobial peptide LL‑37: they kill many harmful bacteria but cause little damage to red blood cells, making them attractive leads for new antibiotics, though they aren’t ready for personal use yet.
Hwang. Young Ji YJ; Jung. Ho Jung HJ; Kim. Min Jung MJ; Roh. Nam Kyung NK; Jung. Jae Wook JW; Lee. Y...
People with psoriasis have higher blood levels of the antimicrobial peptide LL‑37 and several inflammatory signals compared to healthy folks, but the amount of LL‑37 doesn’t change between the two main skin types of psoriasis. The level of these signals goes up as the skin disease gets worse.
Neumann. Ariane A; Berends. Evelien T M ET; Nerlich. Andreas A; Molhoek. E Margo EM; Gallo. Richard...
The study shows that the human antimicrobial peptide LL-37 can help neutrophils (a type of white blood cell) release NETs, which are web-like structures that trap microbes. This effect happens at a concentration of about 5 micromolar and seems to rely on the peptide's oily (hydrophobic) parts. The researchers saw LL-37 move toward the cell nucleus and cause the nuclear membrane to break down, which is a key step in NET formation.
LL-37 is a natural human peptide that can kill a wide range of bacteria, break down harmful biofilms, and help wounds heal. The review says that putting LL-37 on the skin might be a good way to treat infected diabetic foot ulcers, but the evidence is still mostly theoretical and comes from lab studies, not real‑world trials.
LL-37 is a small protein your body makes to fight germs, but recent research shows it can also stir up inflammation and may play a role in autoimmune diseases like rheumatoid arthritis, lupus, and even heart plaque buildup. The review explains how this peptide and its mouse version affect immune pathways and could worsen or trigger these conditions.
The study found that the body’s own protein actin can latch onto the antimicrobial peptide LL‑37, shielding it from being broken down by enzymes released by harmful bacteria like Pseudomonas and Porphyromonas. This protection lets LL‑37 keep killing microbes even in infected areas where those bacterial enzymes are present.
Greer. Ara A; Zenobia. Camille C; Darveau. Richard P RP
This review explains that LL‑37 and other antimicrobial peptides help protect the gums by killing bacteria and also by guiding immune cells, keeping the mouth’s lining healthy. It mainly describes how these proteins work in the gum tissue, not new ways to use them as supplements.
Ren. Shun X SX; Shen. Jin J; Cheng. Alfred S L AS; Lu. Lan L; Chan. Ruby L Y RL; Li. Zhi J ZJ; Wang....
A short piece of the human immune peptide LL-37, called FK-16, can kill colon cancer cells in a dish by triggering two kinds of cell death that don’t need the usual caspase enzymes. It works through the p53‑Bax/Bcl‑2 pathway and the two death routes help each other out. However, the work is only in cell culture, with no dosing or safety data for people.
Jacob. Binu B; Park. Il-Seon IS; Bang. Jeong-Kyu JK; Shin. Song Yub SY
Scientists tweaked a tiny piece of the human immune peptide LL-37 to make new versions that can kill tough bacteria like MRSA and calm down harmful inflammation without hurting human cells in lab tests. While promising, these findings are still early‑stage and not ready for personal use.
Scientists used a special light technique to watch how the natural antimicrobial peptide LL‑37 sticks to and disrupts cell membranes at realistic low levels. They found that the way LL‑37 interacts depends on the types of fats in the membrane, and that cholesterol makes it harder for the peptide to punch holes in the membrane.
Svensson. D D; Westman. J J; Wickström. C C; Jönsson. D D; Herwald. H H; Nilsson. B-O BO
The study shows that a naturally occurring peptide called p33 can stop a harmful antimicrobial peptide, LL-37, from damaging bone‑forming cells (osteoblasts). In lab tests, p33 blocked cell leakage and calcium spikes caused by LL-37, keeping the cells alive.
Säll. Johanna J; Carlsson. Martin M; Gidlöf. Olof O; Holm. Anders A; Humlén. Johan J;...
LL-37, a natural antimicrobial peptide, was found to kill human bone‑like cells (osteoblasts) at low micromolar levels by triggering programmed cell death, and it raises internal calcium through a pathway that doesn’t use the usual voltage‑gated channels. The cell‑killing effect happens even when calcium is removed, suggesting the toxicity isn’t due to calcium overload.
Lofton. Hava H; Pränting. Maria M; Thulin. Elisabeth E; Andersson. Dan I DI
The study shows that bacteria can quickly become resistant to the natural antimicrobial peptide LL‑37 (and similar peptides) through specific genetic changes. While resistant bugs often grow slower, they can still outgrow normal bacteria at low peptide levels like those found in the body, meaning resistance could stick around. This mainly warns that using LL‑37 as a regular antimicrobial could encourage resistant strains.
Chow. Leola N Y LN; Choi. Ka-Yee Grace KY; Piyadasa. Hadeesha H; Bossert. Maike M; Uzonna. Jude J; K...
A small piece of the human immune protein LL‑37, called IG‑19, was given to mice with a rheumatoid‑arthritis‑like disease and it lowered joint damage, inflammation and disease‑related antibodies. The same effect wasn’t seen with a similar peptide from cows. The work is still in animals, so it’s not a ready‑to‑use treatment for people yet.