An antimicrobial peptide of the cathelicidin family that provides innate immune defense by killing pathogens and modulating inflammation and wound healing.
de la Fuente-Núñez. César C; Korolik. Victoria V; Bains. Manjeet M; Nguyen. Uyen U; B...
Scientists found a tiny synthetic peptide (9 amino acids long) that can stop harmful bacteria from forming protective biofilms at doses far lower than needed to kill the bacteria outright. It works on several nasty bugs, including Pseudomonas, Burkholderia, and Listeria, by messing with their movement and gene activity. While itâs not a readyâtoâuse supplement, it shows that very small, positivelyâcharged peptides might be a new way to fight chronic infections.
Hensel. Jonathan A JA; Chanda. Diptiman D; Kumar. Sanjay S; Sawant. Anandi A; Grizzle. William E WE;...
Researchers found that the antimicrobial peptide LL-37 (and its mouse version CRAMP) is higher in prostate cancer tissue and that lowering its levels in mouse cancer cells slows their growth, invasion, and bloodâvessel formation, leading to smaller tumors in mice.
The study shows that a bacterial enzyme called ZmpA can break down the human antimicrobial peptide LLâ37, while a related enzyme ZmpB cannot. This means that certain infections could neutralize LLâ37âs natural defense role, which is important if youâre thinking about using LLâ37 as a supplement or therapy.
The paper shows that the immuneâboosting peptide LLâ37 can trigger a receptor called P2X7 on macrophages, which then activates an inflammationâdriving complex called the inflammasome, but only after the cells have been âprimedâ first. It also finds that blocking certain kinases can stop this activation, hinting at ways to control inflammation.
Li. Guiming G; Domenico. Joanne J; Jia. Yi Y; Lucas. Joseph J JJ; Gelfand. Erwin W EW
The study shows that in mouse mast cells, the antimicrobial peptide similar to human LLâ37 (called CRAMP) is turned on by the NFâÎșB pathway when the cells detect bacterial components, while other signaling routes (MAPKs) donât matter much. This means that anything that blocks NFâÎșB could lower LLâ37 levels and possibly weaken innate immunity, but boosting NFâÎșB might raise them.
Frick. Inga-Maria IM; Karlsson. Christofer C; Mörgelin. Matthias M; Olin. Anders I AI; Janjusev...
The study found that a protein called FAF, made by the common skin bacterium Finegoldia magna, helps the bacteria stick to skin layers and form clumps, and importantly, it can block the human antimicrobial peptide LLâ37. This means that the presence of this bacterium could reduce the natural antibacterial action of LLâ37 on the skin.
Kanthawong. Sakawrat S; Nazmi. Kamran K; Wongratanacheewin. Surasakdi S; Bolscher. Jan G M JG; Wuthi...
Scientists tested ten antimicrobial peptides against the bacteria that causes melioidosis and found that the human peptide LLâ37 killed all 24 bacterial isolates, even those resistant to standard antibiotics. This lab result suggests LLâ37 could become a future treatment, but itâs not yet a usable supplement or protocol for everyday use.
The study found that common drugâpumping mechanisms in E.âŻcoli, P.âŻaeruginosa and S.âŻaureus donât help these bacteria dodge the human antimicrobial peptide LLâ37 (or similar peptides). In plain terms, the bacteriaâs usual resistance tricks donât work against LLâ37, so this peptideâs natural killing ability isnât blocked by those pumps.
Benincasa. M M; Mattiuzzo. M M; Herasimenka. Y Y; Cescutti. P P; Rizzo. R R; Gennaro. R R
The study shows that sticky sugarâcoats (polysaccharides) made by lung bacteria like Pseudomonas can block the killing power of the natural antimicrobial peptide LLâ37 and similar peptides, meaning these defenses work less well in infections where such sugars are abundant.
Mattila. Juha-Pekka JP; Sabatini. Karen K; Kinnunen. Paavo K J PK
The study shows that the antimicrobial peptide LLâ37 (and similar peptides) sticks better to cell membranes that contain a specific oxidized fat molecule called PoxnoPC, even when salt levels are high, while normal salty conditions usually reduce this sticking. This effect depends on a chemical reaction between the peptide and the aldehyde part of PoxnoPC. The findings are mostly basic science and donât give direct dosing or usage tips for everyday health hacks.
Scientists used a standard PCR machine to watch how the antimicrobial peptide LLâ37 and another peptide, magaininâŻ2, poke holes in bacterial cells, and they found the two peptides work in different ways.
Dommisch. H H; Vorderwülbecke. S S; Eberhard. J J; Steglich. M M; Jepsen. S S
The researchers developed a lab technique to measure the immune peptide LLâ37 (and related peptides) in the fluid around your gums. They found that people with early gum inflammation have higher LLâ37 levels than healthy gums, suggesting it could serve as a marker for early periodontal issues.
Lemaire. Simon S; Trinh. Thuy-Tiên TT; Le. Hoang-Thanh HT; Tang. Shun-Chii SC; Hincke. Maxwell...
Researchers found that two naturally occurring peptides, H4-(86-100) and histogranin (HNr), can kill a range of bacteria as well as the wellâstudied antimicrobial peptide LLâ37. They work by blocking a bacterial enzyme called DNA gyrase, and their killing power is boosted by ATP but stopped by metabolic toxins. The study was done in testâtube experiments, not in people, so itâs not yet a usable supplement or treatment.
Hosaka. Yoshio Y; Koslowski. Maureen M; Nuding. Sabine S; Wang. Guoxing G; Schlee. Miriam M; Sch...
The study looked at natural antimicrobial proteins in the upper gut and found that the peptide LLâ37 is barely present in the esophagus, stomach, and duodenum, while other defenses like HBD1 and certain defensins are more common. Even though tissue extracts killed bacteria well, they were less effective against Candida, hinting at missing antimicrobial factors.
Pinkenburg. Olaf O; Pfosser. Achim A; Hinkel. Rabea R; Böttcher. Martina M; Dinges. Claudia C;...
A study in rabbits showed that delivering the gene for the antimicrobial peptide LLâ37 using a viral vector (rAAV) helped grow new sideâbranch blood vessels and improve blood flow in a blocked leg, but it didnât increase tiny capillaries and the effect relied on a specific cellâsignaling pathway.
Minami. Masaaki M; Ohmori. Daisuke D; Tatsuno. Ichiro I; Isaka. Masanori M; Kawamura. Yoshiaki Y; Oh...
The study shows that a friendly mouth bacterium (Streptococcus salivarius) makes a substance (BLIS) that can weaken a defense protein (SIC) used by the harmful throat bug (Streptococcus pyogenes). When SIC is reduced, the natural antimicrobial peptide LLâ37 works better against the bad bacteria. This was seen in lab dishes, not in people.
Different versions of the LLâ37 peptide in primates have distinct shapes and how they stick together, which changes how they interact with cell membranes. The monkey version stays as single pieces and can slip deeper into membranes, acting more like a straightâup antimicrobial. The human version tends to clump together, which reduces its direct killing power but may help it influence host cells.
The study shows a new NMR trick that lets scientists see which parts of antimicrobial peptides like LLâ37 stick to cellâlike membranes. It finds that the aromatic phenylalanine spots are especially important for binding, and swapping a key hydrophobic piece for alanine makes the peptide much weaker against bacteria.
Dürr. Ulrich H N UH; Sudheendra. U S US; Ramamoorthy. Ayyalusamy A
LL-37 is the only human cathelicidin peptide and works like a tiny, flexible sword that kills germs, calms inflammation, attracts immune cells, and helps wounds heal. Itâs made in many parts of the body, from skin to gut to immune cells, and its shape (a helix) is key to how it works. The review gathers what we know about its structure and many roles, pointing out that we still need more basic science to turn this knowledge into realâworld health tricks.
Zheng. Y Y; Niyonsaba. F F; Ushio. H H; Nagaoka. I I; Ikeda. S S; Okumura. K K; Ogawa. H H
The study shows that the natural peptide LLâ37 can boost several immune actions of neutrophils: it makes them release more inflammationâsignalling ILâ8, produce reactive oxygen species, and release other antimicrobial proteins called alphaâdefensins. These effects happen through known cellâsignalling pathways (p38 and ERK) and likely involve NADPH oxidase and calcium signals.