An antimicrobial peptide of the cathelicidin family that provides innate immune defense by killing pathogens and modulating inflammation and wound healing.
A 63‑year‑old woman kept getting painful lumps (chalazions) on her eyelids even though she didn’t have the usual facial redness of rosacea. Tests showed the protein LL‑37 was present in the eye tissue, and her eye problems cleared up after she took oral antibiotics (doxycycline and azithromycin).
Caterino. Jeffrey M JM; Stephens. Julie A JA; Wexler. Randell R; Camargo. Carlos A CA; Hunold. Kathe...
The study measured levels of several antimicrobial peptides in urine, including LL‑37, and found that age doesn’t change LL‑37 levels, while older people have lower levels of another peptide (hBD‑2). This suggests that simply aging isn’t a reason to expect more or less LL‑37 in urine, and that lower hBD‑2 might be part of why older adults get more UTIs.
Lebedev. Maxim M; Benjamin. Aaron B AB; Kumar. Sathish S; Molchanova. Natalia N; Lin. Jennifer S JS;...
A new lab-made molecule called TM9, which copies the natural peptide LL‑37, was shown to stop a mouse coronavirus from spreading in infected mice. The study used a realistic aerosol infection model and found the drug worked against several virus strains without obvious toxicity, but it was only tested in mice, not people.
Luo. Yinli Y; Nan. Meilan M; Dong. Richeng R; Jin. Qingmei Q; Yuan. Jiachen J; Zhi. Jiahui J; Pi. Lo...
A study tested a mussel‑derived protein (MAP) delivered with tiny needles to treat rosacea, a common facial skin condition. In mice made rosacea‑like using the peptide LL‑37, MAP reduced inflammation and improved skin health. In a small human trial (27 people), the same treatment lessened redness, flushing, and visible blood vessels without noticeable side effects.
People with a severe form of psoriasis called erythrodermic psoriasis have a lot of Staphylococcus aureus on their skin and lower levels of the natural antibiotic peptide LL‑37 in their skin (though blood levels are similar to regular psoriasis). This shortage of LL‑37 may help explain why they get more skin infections.
The study shows that the antimicrobial peptide LL‑37 can turn on a cell‑surface channel called P2X7, which is involved in inflammation and several diseases. This activation isn’t stopped by some P2X7 blockers but is blocked by others that bind the main site. The findings mainly clarify how LL‑37 works at a molecular level, without giving direct advice on using the peptide in humans.
Narh. Julius Kwesi JK; Casillas-Vega. Nestor G NG; Zarate. Xristo X
Scientists created a new hybrid antimicrobial peptide called LL-37_Renalexin by linking two known peptides (LL-37 and Renalexin) with a flexible GS linker and using special carrier proteins to make it easier to produce in bacteria. The purified peptide killed a wide range of harmful bacteria, including MRSA and Klebsiella, at much lower concentrations (10‑33 µM) than the original single peptides (50‑100 µM).
Scientists discovered that exposing stem cells to tiny amounts of certain antibiotics makes the cells produce more natural antimicrobial peptides like LL‑37, which helps kill tough bacteria such as MRSA and Pseudomonas. While this shows a possible way to boost the body's own defenses, the method involves lab‑grown stem cells and isn’t something you can directly apply at home yet.
The study shows that the natural peptide LL‑37 can make melanoma skin cancer cells and nearby immune cells more aggressive, helping the tumor grow and spread by boosting factors that build new blood vessels.
Kato. Hiroki H; Ohta. Kouji K; Akagi. Misaki M; Fukada. Shohei S; Sakuma. Miyuki M; Naruse. Takako T...
The study shows that the natural peptide LL‑37 can grab onto double‑stranded RNA, pull it into mouth‑lining cells, and crank up an immune signal called CXCL10 through a sensor named RIG‑I. This effect depends on the RNA and the RIG‑I pathway, and blocking RIG‑I reduces the response.
LL-37 is a natural human peptide that can stop many harmful bacteria from forming protective biofilms, which are tough to treat. It works by blocking the bacteria from sticking together, turning off biofilm‑related genes, messing with their communication signals, breaking down the slime they produce, and killing the bacteria inside the biofilm. However, real‑world safety and dosing data in people are still missing, so it’s not ready for DIY use yet.
Masadeh. Majed M MM; Alshogran. Haneen H; Alsaggar. Mohammad M; Sabi. Salsabeel H SH; Al Momany. Ena...
Researchers created a new peptide called HLM by mixing parts of two natural antimicrobial proteins. In lab tests it killed both regular and antibiotic‑resistant bacteria, including those living in biofilms, at low micromolar concentrations and showed little damage to red blood cells. It also worked together with some common antibiotics, but it showed modest toxicity to mammalian cells, so it isn’t ready for self‑use yet.
Leite. Michel Lopes ML; Duque. Harry Morales HM; Rodrigues. Gisele Regina GR; da Cunha. Nicolau Brit...
This review explains that the LL‑37 part of the cathelicidin family of natural antimicrobial peptides may also help control the immune system, and that smaller pieces of LL‑37 (like SK‑24, IV‑20, FK‑13) could be the parts that talk to human receptors. It doesn’t give new experimental data or dosing advice, just a conceptual overview.
Ridyard. Kylen E KE; Elsawy. Mariam M; Mattrasingh. Destina D; Klein. Darien D; Strehmel. Janine J;...
The study shows that the human antimicrobial peptide LL‑37 works much better against E. coli and P. aeruginosa when paired with the antibiotic polymyxin B, even against drug‑resistant strains and biofilms, and it still works in a simple worm infection model.
Scientists found that mixing a virus‑derived enzyme (Ply2660) with a natural human peptide (LL‑37) kills drug‑resistant Enterococcus faecalis bacteria better than either one alone, both in lab dishes and in infected mice.
Li. Xialin X; Huang. Xingyu X; Li. Long L; Wu. Jiayi J; Yi. Weihong W; Lai. Yuxiao Y; Qin. Lei L
Scientists created a 3‑D‑printed, porous scaffold that slowly releases the human antimicrobial peptide LL‑37. In rats with infected bone gaps, the high‑dose version killed common bacteria like Staph aureus and E. coli, didn’t harm bone‑marrow stem cells, and helped new bone grow, performing as well as vancomycin. The study shows LL‑37 could be a non‑antibiotic way to treat bone infections, but it’s still early animal work and not ready for home use.
Bhattacharjya. Surajit S; Zhang. Zhizhuo Z; Ramamoorthy. Ayyalusamy A
LL-37 is a natural 37‑amino‑acid peptide that helps our bodies fight infections, calm inflammation, attract immune cells, heal wounds, and may even protect against cancer and harmful protein clumps linked to diseases like Alzheimer’s. Scientists are studying its shape and how it works so they can design new drugs based on it, but the review doesn’t give specific ways to use LL‑37 right now.
Scientists created a thin, fiber‑based sheet coated with a plant compound (tannic acid) and the LL‑37 peptide. The coating kills mouth bacteria, calms inflammation, and helps bone cells grow, but the plant coating alone can be toxic to cells. Adding LL‑37 makes the material safer and boosts stem‑cell activity and blood‑vessel formation, leading to better bone healing in animal tests. This is a lab‑level material, not a DIY supplement or protocol.
Scientists used a tiny hole sensor, mass‑spectrometry, and computer simulations to see how short pieces of the immune peptide LL‑37 stick together. They showed these fragments can form small clusters (oligomers), measured how stable those clusters are, and explained the motions that keep them together. The work is mostly about basic science, not a new supplement or dosage tip.
In rats that were overheated to mimic heat stroke, giving the natural antimicrobial peptide LL‑37 helped keep the gut lining intact, lowered inflammation and nitrosative stress, and improved survival. The peptide protected gut cells that make mucus and boosted protective proteins, which together reduced leakage of harmful substances into the bloodstream.