An antimicrobial peptide of the cathelicidin family that provides innate immune defense by killing pathogens and modulating inflammation and wound healing.
Choi. Ka-Yee G KY; Napper. Scott S; Mookherjee. Neeloffer N
The study shows that the natural antimicrobial peptide LL‑37 and a shorter version called IG‑19 can calm down inflammation caused by a protein called IL‑32 in human immune cells. They cut down harmful signals like TNF‑α and IL‑1β while boosting an anti‑inflammatory signal (IL‑1RA), and they do this by tweaking specific cell‑signaling pathways.
The study shows that low doses of the natural peptide LL‑37 can stop a harmful mouth bacterium from forming protective biofilms and makes it easier for immune cells to eat and kill the bugs, even though the bacteria can resist being directly killed by the peptide. This links low LL‑37 levels to gum disease and hints that boosting LL‑37 might improve oral health.
Currie. Silke M SM; Findlay. Emily Gwyer EG; McHugh. Brian J BJ; Mackellar. Annie A; Man. Tian T; Ma...
The human antimicrobial peptide LL‑37 can stop RSV, a common cold‑like virus, from killing lung cells in lab dishes and cuts down the amount of new virus made. A smaller piece of the peptide works too, hinting that a drug could be built from it. While this is only an early‑stage lab result, it suggests that boosting LL‑37 naturally or using a synthetic version might help protect against RSV in the future.
Ruan. Yang Y; Shen. Tao T; Wang. Yan Y; Hou. Man M; Li. Jian J; Sun. Tieying T
The study shows that the human peptide LL‑37 can calm down inflammation caused by a bacterial component (LTA) in immune cells by blocking certain signaling pathways and lowering inflammatory chemicals like TNF‑α and IL‑6.
Jiang. Weiyu W; Sunkara. Lakshmi T LT; Zeng. Xiangfang X; Deng. Zhuo Z; Myers. Sarah M SM; Zhang. Gu...
The study found that certain medium‑chain fatty acids (especially valerate, hexanoate, and heptanoate) boost the body’s natural antimicrobial peptide LL‑37 more than the commonly‑studied butyrate, and that some chemically tweaked versions work just as well. This suggests these compounds could be used as dietary supplements to enhance immune defenses, though the work was done in cell cultures, not people.
Human antimicrobial peptides like LL-37 are natural proteins that help our immune system kill microbes. LL-37 works by inserting into bacterial membranes and forming pores, which destroys the bugs. Its production can be boosted by things like vitamin D, zinc, calcium, short‑chain fatty acids, and UV‑B light, suggesting simple ways to enhance innate immunity.
The study shows that two natural antimicrobial peptides, LL‑37 and human beta‑defensin‑3, work together to calm down inflammation in a lab model of gum tissue. When used together at low, non‑toxic doses, they cut down several key inflammatory signals more than either peptide alone.
Pazgier. Marzena M; Ericksen. Bryan B; Ling. Minhua M; Toth. Eric E; Shi. Jishu J; Li. Xiangdong X;...
The study shows that the extra piece attached to the human antimicrobial peptide LL‑37 (called the cathelin‑like domain) doesn’t kill bacteria by itself and doesn’t stop the active LL‑37 from working, while the whole unprocessed protein still kills Gram‑negative bugs as well as the short LL‑37 peptide does.
Lee. Won Yong WY; Savage. Justin R JR; Zhang. Jianxing J; Jia. Wanjian W; Oottamasathien. Siam S; Pr...
The study shows that the antimicrobial peptide LL-37 can damage bladder cells by causing them to die and release ATP, which fuels inflammation. A specially altered sugar molecule called GM-0111, and other similar GAG compounds, can block this damage in lab cells and mice. This points to a possible way to protect the bladder, but the research is still early and not ready for home use.
Uchio. Eiichi E; Inoue. Hirotoshi H; Kadonosono. Kazuaki K
LL-37, a natural antimicrobial peptide, can block the growth of several eye‑infecting adenoviruses in lab cells at micromolar levels, but it doesn’t work against one type (HAdV4) and the study only tested cells, not people.
The study shows that the natural way LL‑37 peptides stick together (oligomerize) changes how well they kill microbes and how they affect human cells. Different dimer shapes (parallel vs antiparallel) can make the peptide more or less potent and more or less toxic. Researchers also created a special version of LL‑37 that can be “locked” together with UV light to see how it groups in solution and membranes.
The antimicrobial peptide LL-37 can kill Staphylococcus aureus both outside and inside cells at very low (nanomolar) doses, far more potent than common antibiotics, which need much higher concentrations. It works faster and even better against a clinical strain than a lab strain, suggesting it could help clear stubborn infections that hide inside cells.
Sakoulas. George G; Okumura. Cheryl Y CY; Thienphrapa. Wdee W; Olson. Joshua J; Nonejuie. Poochit P;...
The study shows that adding the antibiotic nafcillin can make MRSA bacteria more vulnerable to the body’s natural antimicrobial peptide LL‑37 and other immune defenses, leading to better killing of the bugs in lab tests and in mice. This suggests that nafcillin could be used alongside other antibiotics for hard‑to‑treat MRSA infections, but the evidence is still early and mainly from lab and animal work.
The study found that lactose, the sugar in breast milk, can turn on the gene that makes the antimicrobial peptide LL‑37 in gut cells. This effect works through a specific cellular pathway (p38) and is stronger when combined with compounds like butyrate that are produced by gut bacteria. While the research was done in lab cells, it hints that eating lactose could help boost gut immunity, especially if you also support butyrate production with fiber‑rich foods.
The healthy cornea stays clear of Pseudomonas infection because tears and the surface cells work together, releasing natural antibiotics like LL‑37 and other peptides that kill or block the bacteria. Wearing contact lenses can trap bacteria and tear fluid against the eye, weakening these defenses and letting the bugs attach, invade, and form biofilms.
Parra. Marcela M; Liu. Xia X; Derrick. Steven C SC; Yang. Amy A; Tian. Jinhua J; Kolibab. Kristopher...
The study shows that a TB vaccine (BCG) can boost the body’s natural antimicrobial peptide LL‑37 in mice, and that LL‑37 can lower malaria parasite levels when the parasites are exposed to it. This suggests LL‑37 has some anti‑malaria activity, but the work is done in mice and involves pre‑treating the parasites, not a practical human treatment yet.
Roider. Elisabeth E; Ruzicka. Thomas T; Schauber. Jürgen J
The paper explains that a weak skin barrier in eczema and other allergies is partly due to low levels of the natural antibiotic peptide LL‑37. Vitamin D and UVB light can boost LL‑37 production, which might improve skin protection and lower allergy risk. For DIY health enthusiasts, this suggests that maintaining good vitamin D status (through sunlight or supplements) could be a simple way to support skin health.
Vitamin D (the active form 1,25‑OH2D3) triggers immune cells to make more of the natural antibiotic peptide LL‑37, which then helps the cells kill a TB‑like bacteria by boosting their internal recycling system (autophagy). Adding either vitamin D or synthetic LL‑37 cuts bacterial growth in lab‑grown monocytes, and blocking autophagy stops this benefit.
The study found that the antimicrobial peptide LL-37 (and also LEAP-2 and RNase7) are normally present in tonsils, but people with seasonal allergic rhinitis have lower levels of LEAP-2 and RNase7. Adding LL-37 or LEAP-2 to immune cells in the lab reduced an anti‑inflammatory signal (IL‑10), hinting these peptides can modulate immune responses.
The study shows that the natural antimicrobial peptide LL‑37 can boost the power of common antibiotics against stubborn Pseudomonas aeruginosa biofilms. When LL‑37 (or a similar peptide called CAMA) is added at a low dose, the amount of antibiotic needed to kill the biofilm drops up to eight‑fold, and the combination can also stop the bacteria from sticking to surfaces and forming new biofilms.