An antimicrobial peptide of the cathelicidin family that provides innate immune defense by killing pathogens and modulating inflammation and wound healing.
Srivastava. Meenu M; Chandra. Abhijit A; R. Rahul R; Nigam. Jaya J; Rajan. Pritheesh P; Parmar. Deve...
The study shows that the fatty tissue in the abdomen (the omentum) naturally makes the antimicrobial peptide LL‑37 and other immune‑boosting molecules, and that their production spikes when there’s an infection after surgery.
Bhusal. Anup A; Nam. Youngpyo Y; Seo. Donggun D; Rahman. Md Habibur MH; Hwang. Eun Mi EM; Kim. Seung...
The study shows that the antimicrobial peptide LL-37 (called CRAMP in mice) gets higher in the spinal cords of mice with a MS‑like disease and in human MS brain tissue. Adding more LL-37 makes the disease start sooner and get worse, while reducing its levels helps the mice feel better. The peptide works by talking to microglia (brain immune cells) through a receptor called FPR2 and turning on an inflammation pathway.
Lohova. Elizabeta E; Vitenberga-Verza. Zane Z; Kazoka. Dzintra D; Pilmane. Mara M
The study examined healthy human lungs and found that the antimicrobial peptide LL‑37, along with other defensins and the immune signal IL‑17A, are naturally produced in lung tissues—especially in cartilage, the lining of air sacs, and immune cells—showing they help keep lungs protected from infection.
Roy. Saptarshi S; Alkanfari. Ibrahim I; Chaki. Shaswati S; Ali. Hydar H
The study shows that the peptide LL-37 can trigger skin inflammation similar to rosacea by activating mast cells through a receptor called MRGPRX2 (or MrgprB2 in mice). Mice that lack this receptor or lack mast cells have far less inflammation, and removing a helper protein called β‑arrestin‑2 also reduces the reaction.
Morroni. Gianluca G; Sante. Laura Di LD; Simonetti. Oriana O; Brescini. Lucia L; Kamysz. Wojciech W;...
The study found that the natural antimicrobial peptide LL‑37 can kill tough, drug‑resistant E. coli bacteria and works even better when paired with the antibiotic colistin. Together they stopped bacterial growth faster and also lowered the bacteria's ability to form protective biofilms. However, colistin is a powerful drug with serious side effects, and LL‑37 isn’t available as a safe supplement, so the findings are more about future medical treatments than something you can try at home now.
Zhu. Yanyu Y; Liu. Lei L; Mustafi. Mainak M; Rank. Leslie A LA; Gellman. Samuel H SH; Weisshaar. Jam...
The study shows that certain synthetic, highly charged nylon‑3 polymers can quickly get inside E. coli bacteria and make the bacterial DNA stiff, acting much like the natural peptide LL‑37. Shorter polymers and another peptide, cecropin A, don’t do this as well. The long polymers also cause the bacterial DNA to clump together after about half an hour, hinting at a new way they might kill microbes.
The paper uses computer models to show that the natural human peptide LL‑37 might stick to the part of the coronavirus that binds our cells, and that vitamin D can boost LL‑37 levels, which could help prevent or lessen COVID‑19, but it doesn’t give real‑world dosing or safety data for using the peptide itself.
Scientists trimmed the human immune peptide LL‑37 down to a tiny version and added a fatty tail, creating a short molecule called C10‑KR8d that kills a wide range of bacteria, stops biofilm formation, and even helps the immune system in mouse tests, but it’s still far from being a safe, approved supplement for people.
LL-37 is a natural human peptide that helps fight bacteria. Researchers have discovered it can change shape and join together in many forms, which lets it stick to different bacterial parts like membrane lipids and LPS. This structural knowledge could help design stronger, more stable antimicrobial peptides, but the paper doesn’t give any direct dosing or usage tips for everyday use.
Kulkarni. Nikhil N NN; O'Neill. Alan M AM; Dokoshi. Tatsuya T; Luo. Elizabeth W C EWC; Wong. Gerard...
Scientists studied the human peptide LL‑37 and found that changing certain building blocks on its oily side stops it from causing inflammation by handing over RNA to cell surface receptors, while still keeping its ability to kill microbes. This means the inflammatory effect of LL‑37 can be separated from its antimicrobial action.
Toor. Himanshu G HG; Banerjee. Devjani I DI; Chauhan. Jenabhai B JB
A computer study shows the natural peptide LL‑37 can stick tightly to a toxin (PVL) made by drug‑resistant Staph bacteria, better than some chemicals that have been tested before, and it looks safe in the body, but this is only a virtual test and not proven in real life yet.
The study shows that the natural peptide LL‑37 can trigger skin inflammation similar to rosacea by turning on a cellular alarm called the NLRP3 inflammasome. It gets inside immune cells via a P2X7 channel, messes up lysosomes, and then activates inflammatory signals. Mice lacking NLRP3 or treated with an NLRP3 blocker showed much less skin damage, proving the pathway is key.
The study found that the natural peptide LL‑37 is reduced in liver cancer tissue, and when a lab‑made version is added to liver cancer cells it slows their growth and lowers inflammation signals, but it doesn’t kill the cells outright. These effects were seen in cell‑culture experiments, not in people.
In a mouse study, drinking water with 15% gum Arabic for four weeks raised the levels of the immune‑boosting peptide cathelicidin (the mouse version of human LL‑37) in immune cells, while a higher 30% dose did not show a clear benefit. The effect seems to depend on the amount of gum Arabic, but the work was done in mice, not people.
Researchers made a version of the natural immune peptide LL‑37 that can’t be changed by the body’s PAD enzymes during inflammation. This new version, called hArg‑LL‑37, kills bacteria just as well as the original and still helps control inflammation, even when PAD enzymes are active. It breaks down at the same rate as the normal peptide, so it’s stable enough for potential therapeutic use.
Patiño. Maria Isabel MI; Restrepo. Luz Marina LM; Becerra. Natalia Yiset NY; van der Mei. Henny...
Scientists made a lab‑grown skin model that was genetically tweaked to produce the natural antimicrobial peptide LL‑37. The modified skin grew better and was able to kill common wound bacteria like Staph aureus more effectively than normal skin. This shows LL‑37 has real potential to help wounds heal and stay infection‑free, but the technique used (gene‑delivery to skin cells) isn’t something you can do at home yet.
Quemé-Peña. Mayra M; Ricci. Maria M; Juhász. Tünde T; Horváti. Kata K; B&#x...
Researchers found that the drug suramin can stick to the immune peptide LL-37 and change its shape, which makes LL-37 less likely to kill cells in lab tests. This suggests a way to dial down the harmful side‑effects of too much LL-37, but the study was done in cells and used a drug with its own safety concerns.
Plataki. Marina N MN; Vamvoukaki. Rodanthi R; Samonis. George G; Bikis. Charalampos C; Gorgomiti. Ma...
In people with type‑2 diabetes, about a third carry Staph aureus in their noses. Low vitamin D is common, but taking extra vitamin D didn’t reduce this bacterial carriage. Interestingly, the antimicrobial peptide LL‑37 was actually higher in those who were carriers, suggesting the body may boost LL‑37 in response to the bacteria.
Aidoukovitch. Alexandra A; Bankell. Elisabeth E; Davies. Julia R JR; Nilsson. Bengt-Olof BO
The paper shows that the natural antimicrobial peptide LL‑37 found in saliva is too low to kill the cavity‑causing bacteria Streptococcus mutans, but adding synthetic LL‑37 at high micromolar levels (8‑10 µM) can kill S. mutans while leaving the friendly S. gordonii untouched. However, achieving such concentrations in the mouth with everyday products is difficult, so the finding is more of a proof‑of‑concept than a ready‑to‑use hack.
The study tested a human antimicrobial peptide called LL‑37 and some common antifungal drugs against Candida fungi that form tough biofilms. LL‑37 didn’t work against the fungal biofilms, but a drug combo of fluconazole and caspofungin showed a helpful synergistic effect in about 60% of the samples. Other drug combos were mostly ineffective or even counter‑productive.