An antimicrobial peptide of the cathelicidin family that provides innate immune defense by killing pathogens and modulating inflammation and wound healing.
Nell. Marja J MJ; Tjabringa. G Sandra GS; Wafelman. Amon R AR; Verrijk. Ruud R; Hiemstra. Pieter S P...
Researchers made new short versions of the human peptide LL-37, especially one called P60.4, that can neutralize bacterial toxins (LPS and LTA) as well as the original peptide but cause less inflammation, and the chemically tweaked version appears safe and still kills microbes.
Bucki. Robert R; Namiot. Dorota B DB; Namiot. Zbigniew Z; Savage. Paul B PB; Janmey. Paul A PA
The study found that the natural antimicrobial peptide LL-37 (and its synthetic copy WLBU2) gets stuck to the sticky proteins (mucins) in saliva, which blocks their ability to kill bacteria. A different antimicrobial molecule, the cationic steroid CSA-13, keeps working even when mixed with the same amount of saliva.
Barańska-Rybak. W W; Sonesson. A A; Nowicki. R R; Schmidtchen. A A
The study shows that natural sugars called glycosaminoglycans (found in wound fluid, plasma, and serum) can block the infection‑killing action of the human peptide LL‑37, but positively charged substances like chitosan can free LL‑37 and make it work better again.
The skin not only acts as a physical barrier but also makes natural antimicrobial proteins like LL‑37, beta‑defensins, and lysozyme that kill germs and help heal wounds. These molecules also influence inflammation and cell growth, and some are being tested as new skin infection treatments. While the paper is a review, it confirms that boosting these peptides could support skin health and immunity.
Li. Xia X; Li. Yifeng Y; Han. Huiyun H; Miller. Donald W DW; Wang. Guangshun G
Researchers mapped which parts of the human antimicrobial peptide LL-37 actually do the work. They found the short 13‑amino‑acid piece (positions 17‑29) kills bacteria and cancer cells, and swapping some parts to D‑amino acids keeps the killing power but makes it less harmful to human cells. This shows a tiny, safer version of LL‑37 could be made, but it’s still early‑stage lab work.
Neville. Frances F; Cahuzac. Marjolaine M; Konovalov. Oleg O; Ishitsuka. Yuji Y; Lee. Ka Yee C KY; K...
The study shows that the human peptide LL‑37 can poke into and break apart membranes that look like bacterial cells while leaving membranes that look like human cells untouched, meaning it kills bacteria without damaging our own cells.
Scientists figured out a way to make the human antimicrobial peptide LL‑37 in bacteria, label it for detailed studies, and pull it out using a simple formic‑acid cut. The lab‑made peptide works just as well as the chemically‑synthesized version, and the technique can be used for other small peptides that have an Asp‑Pro link.
Sieprawska-Lupa. Magdalena M; Mydel. Piotr P; Krawczyk. Katarzyna K; Wójcik. Kinga K; Puklo. Ma...
The study shows that the human antimicrobial peptide LL‑37 gets chopped up and inactivated by a Staphylococcus aureus enzyme called aureolysin, while another bacterial enzyme (V8 protease) only cuts off the front part, leaving a shorter piece (LL‑17‑37) that still kills the bacteria. This means the full‑length peptide may lose its power against S. aureus that makes aureolysin, but the C‑terminal fragment stays active.
Ciornei. Cristina D CD; Sigurdardóttir. Thorgerdur T; Schmidtchen. Artur A; Bodelsson. Mikael M
Researchers compared the natural antimicrobial peptide LL-37 to shorter versions (106 and 110) and a more hydrophobic version (LLKKK). All versions killed bacteria and fungi and blocked harmful bacterial toxins, but the shorter pieces were far less damaging to human cells and kept working even when serum was present, unlike the full‑length LL-37. The overly hydrophobic LLKKK was actually more toxic to blood cells.
Soehnlein. Oliver O; Zernecke. Alma A; Eriksson. Einar E EE; Rothfuchs. Antonio Gigliotti AG; Pham....
In mice, a protein called LL-37 released by neutrophils (a type of white blood cell) helps pull in a second wave of immune cells called inflammatory monocytes. This recruitment boosts overall inflammation signals and improves the body's ability to clear bacteria.
Murakami. Masamoto M; Lopez-Garcia. Belen B; Braff. Marissa M; Dorschner. Robert A RA; Gallo. Richar...
After being released onto the skin, the body’s LL‑37 protein gets cut up by enzymes into several smaller pieces. These new pieces kill skin bugs like Staph and yeast even better than the original LL‑37, but they no longer trigger the skin cells to release the inflammation signal IL‑8. So the same gene can produce a version that’s more focused on killing microbes and less on causing inflammation.
Braff. Marissa H MH; Hawkins. Mi'i A MA; Di Nardo. Anna A; Lopez-Garcia. Belen B; Howell. Michael D...
The study shows that the skin‑protective peptide LL‑37 has two separate jobs: some parts kill microbes, while other parts trigger inflammation by making cells release IL‑8. These two actions don’t line up – you can have strong antimicrobial effects without causing a big immune response, and vice‑versa. Cutting the peptide into smaller pieces changes which job dominates, so you could pick fragments that suit your goal (e.g., anti‑infection vs. low‑irritation).
Wah. Jenny J; Wellek. Anne A; Frankenberger. Marion M; Unterberger. Pia P; Welsch. Ulrich U; Bals. R...
The study shows that the antimicrobial peptide LL‑37 (along with other defensins) is naturally made by immune cells like T‑cells, B‑cells, and macrophages in the lungs and gut, not just by the lining cells. This means LL‑37 likely helps the body’s own defenses in many ways beyond just killing microbes on surfaces.
Dorschner. Robert A RA; Lopez-Garcia. Belen B; Peschel. Andreas A; Kraus. Dirk D; Morikawa. Kazuya K...
The study shows that the natural antimicrobial peptide LL‑37 can kill bacteria like Staph and E. coli at normal salt levels, but only when carbonate (like bicarbonate) is present. Without carbonate, the peptide looks inactive. Bacteria adapt to carbonate‑rich environments by changing their cell wall and stress‑response genes, which makes them more vulnerable to LL‑37.
Zughaier. Susu M SM; Shafer. William M WM; Stephens. David S DS
The study shows that the antimicrobial peptide LL‑37 can calm down inflammation caused by bacterial toxins by lowering TNF‑alpha and nitric‑oxide release, but at the same time it makes immune cells fire off more reactive oxygen species (ROS), a kind of oxidative burst. This boost in ROS happens even when the usual toxin‑sensing pathway (TLR4) is missing, meaning LL‑37 acts directly on the cell’s ROS‑producing machinery.
Carlsson. Göran G; Wahlin. Ylva-Britt YB; Johansson. Anders A; Olsson. Anders A; Eriksson. Torb...
Even when people with severe congenital neutropenia get normal white‑blood‑cell counts from G‑CSF, they can still develop bad gum disease because their neutrophils lack the antimicrobial peptide LL‑37. This suggests that just fixing cell counts isn’t enough for oral health in these patients.
López-García. Belén B; Lee. Phillip H A PH; Gallo. Richard L RL
The human peptide LL‑37 can kill common skin‑fungi that cause athlete's foot, ringworm and yeast‑type rashes at low micromolar levels, and skin naturally makes more of it when infected. This suggests LL‑37 helps protect skin, but the study only tested it in the lab, not in real‑world products.
LL-37 is a natural antimicrobial peptide in skin that helps keep you from infections. It’s made more when skin is inflamed or when certain signals like vitamin D are present, and low levels are linked to skin problems like eczema.
López-García. Belén B; Lee. Phillip H A PH; Yamasaki. Kenshi K; Gallo. Richard L RL
LL-37, a natural human peptide, can kill the fungus Candida albicans on the skin, especially when it’s broken down into smaller pieces like RK‑31 and when the environment mimics sweat. It works by poking holes in the fungal membrane, but it doesn’t seem to protect the body from deeper infections. This means it could be useful as a topical antifungal, but it isn’t a cure for systemic yeast problems.
Bowdish. Dawn M E DM; Davidson. Donald J DJ; Scott. Monisha G MG; Hancock. Robert E W RE
The study shows that the human peptide LL‑37 and a smaller peptide called indolicidin can calm down inflammation caused by bacterial toxins, even if they’re added after the toxin hits cells. They work even better together at low doses, but another similar peptide, Bac2A, doesn’t have this anti‑inflammatory effect and instead attracts immune cells. While interesting, the findings don’t give clear dosing or safety info for personal use.