An antimicrobial peptide of the cathelicidin family that provides innate immune defense by killing pathogens and modulating inflammation and wound healing.
People with adult T‑cell leukemia/lymphoma have weaker skin defenses because their immune cells that normally trigger antimicrobial peptides like LL‑37 are reduced, leading to more frequent fungal skin infections.
Jendeberg. Anna Lange AL; Strålin. Kristoffer K; Hultgren. Olof O
In people with community‑acquired pneumonia, two antimicrobial proteins (SLPI and BPI) go up in the blood, but LL‑37 – the peptide many biohackers talk about – does not. The rise in SLPI was bigger in men than women, and none of these proteins predicted how sick someone got or what bug caused the infection.
The study tested different fluorescent dyes to watch bacterial DNA in real time and found that some dyes meant for dead cells actually work well on live bacteria without harming them. When they looked at two antimicrobial peptides, they saw that cecropin A scrambled the normal separation of DNA and ribosomes inside E. coli, but the human peptide LL‑37, even though it can poke holes in the bacterial membrane, did not cause this internal disruption.
Sakoulas. George G; Bayer. Arnold S AS; Pogliano. Joseph J; Tsuji. Brian T BT; Yang. Soo-Jin SJ; Mis...
Adding the antibiotic ampicillin makes another drug, daptomycin, work better against a hard‑to‑kill bacteria (VRE) and also makes the bacteria more vulnerable to natural antimicrobial peptides like LL‑37.
Scott. Aaron A; Weldon. Sinéad S; Buchanan. Paul J PJ; Schock. Bettina B; Ernst. Robert K RK; M...
LL-37 can stop harmful inflammation caused by bacterial endotoxin (LPS) by binding to it outside cells, but only while it’s present in the surrounding fluid. In cystic fibrosis lungs, DNA and sugary molecules stick to LL-37, blocking this protective effect. Treating the sputum with enzymes that cut DNA and these sugars (DNase and heparinase) frees up LL-37 and restores its ability to neutralize LPS.
Girnita. A A; Zheng. H H; Grönberg. A A; Girnita. L L; Ståhle. M M
The peptide LL‑37 can stick to the IGF‑1 receptor, turn on a specific cell‑signaling route (ERK) and make cancer cells move and invade more, without making them grow faster. This suggests LL‑37 might boost tumor spread rather than help health.
Researchers found that alarin, a brain peptide, can kill the gut bacterium E. coli in lab tests, working about as well as the well‑known antimicrobial peptide LL‑37. It does this without breaking red blood cells, but it only works on gram‑negative bugs like E. coli and not on gram‑positive ones such as Staph.
Researchers found that the natural peptide LL-37 can turn blood monocytes into a new type of bone‑forming cell they call monoosteophils. These cells make bone‑like structures in lab dishes and even in mice, and they show markers of both bone‑building and bone‑breaking cells. While the work is still early‑stage and needs lab equipment, it hints that boosting LL-37 could one day help heal fractures or treat osteoporosis.
Inomata. Megumi M; Into. Takeshi T; Murakami. Yukitaka Y
The body’s own antimicrobial peptide LL‑37 can calm down inflammation in gum cells caused by dead Porphyromonas gingivalis bacteria, lowering levels of IL‑6, IL‑8 and CXCL10 signals that drive gum disease.
LL-37, a natural antimicrobial peptide, can calm down inflammation in gum‑related cells at low doses, but if you use a lot it kills those cells and stops them from dividing. The study was done in a lab dish, not in people, so the results are early and need more testing before any real‑world use.
Montreekachon. P P; Chotjumlong. P P; Bolscher. J G M JG; Nazmi. K K; Reutrakul. V V; Krisanaprakorn...
LL-37, a natural antimicrobial peptide, can trigger inflammation in gum cells by raising IL‑8 levels through the P2X7 receptor and MAP‑kinase pathway, but it isn’t toxic up to 10 µM.
Scientists improved a lab method to make the human antimicrobial peptide LL‑37 in bacteria. By deleting an extra cutting site in the DNA vector, they could cleanly release the peptide from its carrier protein, making it easier to purify a functional product.
LL-37 is a natural human peptide that helps fight infections and heal wounds. This study shows that only a few specific building blocks (especially an arginine at position 23 and a lysine at 25) are crucial for killing the common gut bug E. coli, while other parts are less important. For Staph bacteria, the peptide is less sensitive to single changes.
McGee. David J DJ; George. Alika E AE; Trainor. Elizabeth A EA; Horton. Katherine E KE; Hildebrandt....
The study shows that when the stomach bug Helicobacter pylori grabs cholesterol from the host and adds a sugar to it, it becomes far more resistant to many antibiotics and the natural antimicrobial peptide LL-37. This cholesterol‑driven resistance can be partly undone by mutating bacterial genes that handle cholesterol or lipid A, but the bacteria still stay dangerous in animals.
Villanueva. Eneida E; Yalavarthi. Srilakshmi S; Berthier. Celine C CC; Hodgin. Jeffrey B JB; Khandpu...
The study shows that a special type of neutrophil in lupus patients makes lots of a protein called LL‑37 and throws out web‑like structures (NETs) that damage blood vessels and trigger inflammation. These NETs are found in the skin and kidneys of lupus patients and are linked to higher disease markers. While this explains how LL‑37 may worsen lupus, it doesn’t give direct steps for healthy people to use.
Swidergall. Marc M; Ernst. Andreas M AM; Ernst. Joachim F JF
Candida albicans releases a sugary fragment of a surface protein (called Msb2*) that sticks tightly to the human antimicrobial peptide LL-37 and other similar molecules. When it binds, LL-37 can’t kill the fungus or nearby bacteria as well. The binding works best when the fragment is properly sugar‑coated; if the sugars are missing, the effect drops.
Researchers made tiny silver particles coated with starch and tested them against common germs. The particles killed both Gram‑positive and Gram‑negative bacteria, weren’t toxic to immune cells at the needed dose, helped those cells kill bacteria inside them, and stopped harmful biofilms from forming. They worked better than the natural antimicrobial peptide LL‑37 in these tests.
Robinson. Mark W MW; Donnelly. Sheila S; Hutchinson. Andrew T AT; To. Joyce J; Taylor. Nicole L NL;...
Researchers found that a protein secreted by a liver fluke looks a lot like the human antimicrobial peptide LL‑37 and can stick to bacterial toxin LPS, stopping it from triggering inflammation. In mouse tests, both the full protein and a short piece of it reduced inflammatory signals and protected the animals from LPS‑induced damage, suggesting a new way to calm the immune system.
Schrumpf. J A JA; van Sterkenburg. M A J A MA; Verhoosel. R M RM; Zuyderduyn. S S; Hiemstra. P S PS
The study shows that the asthma‑related cytokine IL‑13 makes airway cells better at turning vitamin D into its active form, which then boosts production of the antimicrobial peptide LL‑37. In simple terms, when IL‑13 is present, taking vitamin D may lead to higher levels of LL‑37, a molecule that helps fight infections in the lungs.
Pompilio. A A; Scocchi. M M; Pomponio. S S; Guida. F F; Di Primio. A A; Fiscarelli. E E; Gennaro. R...
The study tested several cathelicidin peptides, including LL‑37, against bacteria from cystic fibrosis lungs. LL‑37 didn’t kill the bugs at realistic doses, while a few other peptides (SMAP‑29, BMAP‑28, BMAP‑27) showed stronger antibacterial activity than the antibiotic tobramycin, though they’re still early‑stage research.