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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 Jun 7, 2022

Cathelicidin-related antimicrobial peptide promotes neuroinflammation through astrocyte-microglia communication in experimental autoimmune encephalomyelitis.

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.

Utility 2
pubmed Oct 1, 2021

Local Defence System in Healthy Lungs.

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.

Utility 2
pubmed May 26, 2022

Role of MrgprB2 in Rosacea-Like Inflammation in Mice: Modulation by β-Arrestin 2.

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.

Utility 2
pubmed Mar 1, 2021

Synergistic effect of antimicrobial peptide LL-37 and colistin combination against multidrug-resistant <i>Escherichia coli</i> isolates.

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.

Utility 2
pubmed Oct 30, 2021

Local rigidification and possible coacervation of the Escherichia coli DNA by cationic nylon-3 polymers.

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.

Utility 2
pubmed Aug 9, 2021

An in silico scientific basis for LL-37 as a therapeutic for Covid-19.

Lokhande. Kiran Bharat KB; Banerjee. Tanushree T; Swamy. Kakumani Venkateswara KV; Ghosh. Payel P; D...

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.

Utility 2
pubmed Apr 23, 2021

Short and Robust Anti-Infective Lipopeptides Engineered Based on the Minimal Antimicrobial Peptide KR12 of Human LL-37.

Lakshmaiah Narayana. Jayaram J; Golla. Radha R; Mishra. Biswajit B; Wang. Xiuqing X; Lushnikova. Tam...

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.

Utility 2
pubmed May 14, 2021

Structural Plasticity of LL-37 Indicates Elaborate Functional Adaptation Mechanisms to Bacterial Target Structures.

Zeth. Kornelius K; Sancho-Vaello. Enea E

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.

Utility 2
pubmed May 26, 2021

Sequence determinants in the cathelicidin LL-37 that promote inflammation via presentation of RNA to scavenger receptors.

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.

Utility 2
pubmed Oct 13, 2020

<i>In Silico</i> Evaluation of Human Cathelicidin LL-37 as a Novel Therapeutic Inhibitor of Panton-Valentine Leukocidin Toxin of Methicillin-Resistant <i>Staphylococcus aureus</i>.

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.

Utility 2
pubmed Mar 18, 2021

Antimicrobial Peptide LL-37 Drives Rosacea-Like Skin Inflammation in an NLRP3-Dependent Manner.

Yoon. Sung-Hyun SH; Hwang. Inhwa I; Lee. Eunju E; Cho. Hyo-Joung HJ; Ryu. Ju Hee JH; Kim. Tae-Gyun T...

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.

Utility 2
pubmed Mar 6, 2021

Host defense peptide LL-37 is involved in the regulation of cell proliferation and production of pro-inflammatory cytokines in hepatocellular carcinoma cells.

Ding. Xiaohui X; Bian. Dongyan D; Li. Weike W; Xie. Yafeng Y; Li. Xiangyang X; Lv. Jilong J; Tang. R...

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.

Utility 2
pubmed Jun 1, 2022

The effect of gum Arabic supplementation on cathelicidin expression in monocyte derived macrophages in mice.

Siednamohammeddeen. Nagat N; Badi. Rehab R; Mohammeddeen. Tahane T; Enan. Khalid K

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.

Utility 2
pubmed Nov 30, 2020

Citrullination-Resistant LL-37 Is a Potent Antimicrobial Agent in the Inflammatory Environment High in Arginine Deiminase Activity.

Bryzek. Danuta D; Golda. Anna A; Budziaszek. Joanna J; Kowalczyk. Dominik D; Wong. Alicia A; Bieleck...

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.

Utility 2
pubmed Jul 5, 2021

Nonviral Expression of LL-37 in a Human Skin Equivalent to Prevent Infection in Skin Wounds.

Pati&#xf1;o. 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.

Utility 2
pubmed Dec 3, 2020

Old Polyanionic Drug Suramin Suppresses Detrimental Cytotoxicity of the Host Defense Peptide LL-37.

Quem&#xe9;-Pe&#xf1;a. Mayra M; Ricci. Maria M; Juh&#xe1;sz. T&#xfc;nde T; Horv&#xe1;ti. 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.

Utility 2
pubmed May 10, 2021

Vitamin D and Cathelicidin (LL-37) Status in Patients with Type 2 Diabetes and Staphylococcus aureus Nasal Carriage.

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.

Utility 2
pubmed Mar 9, 2021

Exogenous LL-37 but not homogenates of desquamated oral epithelial cells shows activity against <i>Streptococcus mutans</i>.

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.

Utility 2
pubmed Nov 30, 2020

Effect of antifungal agents, lysozyme and human antimicrobial peptide LL-37 on clinical <i>Candida</i> isolates with high biofilm production.

Chen. Yi-Chun YC; Chen. Fang-Ju FJ; Lee. Chen-Hsiang CH

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.