An antimicrobial peptide of the cathelicidin family that provides innate immune defense by killing pathogens and modulating inflammation and wound healing.
Ju. Yinghua Y; Hua. Jian J; Sakamoto. Koji K; Ogawa. Hideoki H; Nagaoka. Isao I
The study shows that glucosamine, a common supplement, can dampen inflammation caused by the antimicrobial peptide LL‑37 in human blood‑vessel cells. It does this by increasing a cellular sugar modification (O‑GlcNAc) that blocks the cells from releasing inflammatory signals (MCP‑1 and ICAM‑1). This suggests glucosamine might help protect blood vessels from inflammation linked to atherosclerosis.
Li. Yi Y; Huang. Junling J; Zhang. Yan Y; He. Yide Y; Cai. Dongxuan D; Xu. Min M; Ma. Qianli Q; Zhan...
Scientists coated titanium used in dental implants with the antimicrobial peptide LL-37, which slowly releases for over a week. This coating helped gum cells grow and stick better while killing common mouth bacteria, leading to a tighter soft‑tissue seal around the implant in rats.
LL-37 is a natural protein that helps fight infections and calm down inflammation. During severe infections like sepsis, its levels in the blood change a lot, and giving extra LL-37 to mice with sepsis helped them live longer. Scientists think that making stable versions of LL-37 could become a new way to diagnose or treat sepsis, but it’s still early‑stage research.
Huang. Wenyue W; He. Hailun H; Wu. Haien H; Wang. Yichong Y; Wang. Jingyu J; Sun. Yan Y; Wang. Hexia...
The study shows that the antimicrobial peptide LL‑37 can trigger skin inflammation in rosacea by activating a protein called STING, and another protein, LAPTM5, makes STING stick around longer, worsening the inflammation. Blocking STING or reducing LAPTM5 levels lessened the skin problems in mice.
Gao. Hu H; Tang. Fajuan F; Chen. Bin B; Li. Xihong X
In mouse and cell experiments, the natural peptide LL‑37 helped protect lung cells from the damage caused by sepsis by cutting down inflammation, oxidative stress, and cell death, mainly through turning on a cleanup process called autophagy and lowering a protein called ZBP1.
The study shows that taking high‑dose vitamin D (the form 1,25‑OH2‑D3) can boost a protein called LL‑37, which then attracts immune cells that actually help liver cancer grow. Adding the drug suramin blocks LL‑37, shifts those immune cells to a cancer‑fighting type, and makes vitamin D work better against tumors in mice. This is all done in cell cultures and mouse models, not in people.
Researchers tested small pieces of the natural skin peptide LL‑37 and related molecules on human skin cells in a dish and found they can reduce UV‑induced damage, lower inflammation, boost antioxidant defenses, help cells move and make more collagen, and even cut down on sugar‑linked aging and melanin production.
The study shows that the brain chemical serotonin makes a skin‑inflammation model caused by the peptide LL‑37 worse, and it does this through a specific receptor called HTR3A. Blocking that receptor with a drug (tropisetron) or gene‑silencing reduced the inflammation in cells and mice.
The study used computer simulations to see how a short piece of the human antimicrobial peptide LL‑37 (positions 17‑29) forms a four‑helix bundle and sticks to cell membranes, especially the negatively charged ones found in bacteria. It shows the bundle binds tightly in a face‑down way, can bend the membrane, and either senses or disrupts different bacterial membranes.
Pennone. Vincenzo V; Meogrossi. Giada G; Carenzi. Giacomo G; Sarlah. David D; Biagiotti. Marco M; Lo...
Researchers made a silk‑based sponge that can hold short pieces of the natural antimicrobial peptide LL‑37 (called FK‑16 and GF‑17) and tested it on antibiotic‑resistant Staph bacteria that cause joint implant infections. The sponge released most of the FK‑16 quickly and kept enough around to kill the MRSE strain, especially when the sponge also contained bone‑growth signals. GF‑17 didn’t release well and didn’t kill the bugs, and neither peptide worked against MRSA in this test.
Cathepsin S is an enzyme that helps the immune system work but can also worsen autoimmune and inflammatory diseases by breaking down important proteins like the antimicrobial peptide LL‑37. Scientists are looking at ways to block cathepsin S to treat these conditions, but current drugs have limitations.
A mouse study showed that putting a non‑psychoactive cannabinoid called cannabigerol (CBG) on the skin reduced redness, swelling, and inflammation that mimic rosacea, likely by calming both immune and blood‑vessel signals. However, the work was done in animals, not people, so it’s an early hint rather than a proven treatment.
The study shows that during Legionella infection neutrophils release DNA traps (NETs) but these traps normally lack the antimicrobial peptide LL‑37, so they don’t stop the bacteria. When patients are treated with the antibiotic clarithromycin, the NETs do pick up LL‑37 and can suppress bacterial growth. This suggests the drug, not the peptide alone, changes how the immune traps work.
Liu. Zhantao Z; Zhang. Qingsong Q; Su. Dan D; Chen. Hong H; Wang. Bowen B; Ye. Lin L; Wang. Peiyan P...
The study shows that the natural peptide LL‑37 (called CRAMP in mice) can protect heart cells from a type of iron‑driven cell death called ferroptosis, which contributes to heart damage after a heart attack. In mouse cells and a mouse heart‑attack model, adding LL‑37 or increasing its production reduced cell death and improved heart function by blocking an enzyme (cathepsin L) that otherwise lowers a protective protein (PDIA4).
Neshani. Alireza A; Zare. Hosna H; Ghiasi. Nooshin Sadat NS; Karimi. Mohammad Ali MA; Hosseini Bafgh...
LL-37 is a natural human peptide that can kill a wide range of germs – over 38 bacteria, 16 fungi and 16 viruses – by breaking their membranes, stopping biofilms and messing with their DNA or viral entry. However, it breaks down quickly in the body and can be toxic at high doses, so it isn’t yet a safe, off‑the‑shelf supplement.
Cerps. Samuel S; Ramu. Sangeetha S; Gidlöf. Olof O; Menzel. Mandy M; Swärd. Karl K; Uller....
The study shows that adding the antimicrobial peptide LL‑37 to human airway cells infected with the common cold virus boosts the cells' production of interferon‑β, a key antiviral signal, and lowers the amount of virus. This boost relies on a rise in calcium inside the cells and needs the virus to be inside endosomes. The work was done in a lab dish, not in people, and uses a synthetic peptide that isn’t a standard supplement.
Włodarczyk. Jakub J; Kamysz. Elżbieta E; Fichna. Jakub J
Researchers tested a short piece of the antimicrobial peptide LL‑37, called KR‑12, and a few chemically tweaked versions, to see if they could kill colon cancer cells and reduce tumors in mice. In lab dishes the peptides were more toxic to cancer cells than to normal colon cells, and when given rectally to mice with chemically induced colon cancer they lowered tumor counts and inflammation. However, the effective doses were relatively high and the work is still at the early animal‑study stage, so it isn’t ready for personal use yet.
Chow. Billy Kwok Chong BKC; Choi. Ye Gi YG; Wong. Trevor K TK; Nawabjan. Shaik Abdullah SA; Li. Kesa...
In mice, a skin‑irritating peptide called LL‑37 creates rosacea‑like redness, swelling, and itching. Blocking the mast‑cell receptor MRGPRX2/B2 with a new compound (GE1111) cuts down these skin problems, lowers inflammation markers, and protects the skin barrier. The effect was seen both in live mice and in cell‑culture tests, showing the drug stops mast cells from over‑reacting with skin cells and immune cells.
This paper reviews how tiny proteins like LL‑37 can mess with bacteria’s “talking” system (quorum‑sensing) so they become less harmful without killing them, which might help fight antibiotic resistance. It explains the science, shows that natural and engineered peptides can block bacterial signals, and notes the big hurdles like making the peptides stable and getting them into the body.
Kapica. Martyna M; Kamysz. Elżbieta E; Grabowska. Ola O; Tesmar. Aleksandra A; Pająk. Ma...
The study examined how two short, fatty‑acid‑linked pieces of the human antimicrobial peptide LL‑37 (C12‑KR12 and C14‑KR12) stick to a negatively charged vanadium cluster (decavanadate). They bind mainly through charge attractions, and the vanadium cluster weakens the peptides’ helical shape, especially when heated.