An antimicrobial peptide of the cathelicidin family that provides innate immune defense by killing pathogens and modulating inflammation and wound healing.
Habes. Chahrazed C; Weber. Günther G; Goupille. Caroline C
LL-37, a peptide known for killing microbes, can also make breast cancer cells move faster by attaching to negatively‑charged sugar chains (sulfated GAGs) on the cell surface, especially through a protein called syndecan‑4. Blocking these sugar chains stops the peptide’s effect, showing that its action isn’t through a classic receptor but through charge‑based binding.
Oliveira Junior. Luiz Roberto de LR; Carvalho. Thaysa Buss TB; Santos. Rodrigo Mattos Dos RMD; Costa...
In people with chronic Chagas disease, those who have heart problems tend to have lower blood levels of vitamin D, but their levels of the antimicrobial peptide LL‑37 are similar to those without heart issues. The study didn't find any link between common vitamin D‑receptor gene variants and disease form.
Enigk. Katharina K; Jentsch. Holger H; Rodloff. Arne C AC; Eschrich. Klaus K; Stingu. Catalina-Suzan...
The study tested five antimicrobial peptides on a range of oral bacteria and a fungus. Nisin was the strongest, stopping many common mouth microbes, while melittin and lactoferrin had limited effects. LL‑37, the peptide you asked about, showed no activity against any of the tested strains.
Armiento. Valentina V; Hille. Kathleen K; Naltsas. Denise D; Lin. Jennifer S JS; Barron. Annelise E...
Scientists found that the natural human peptide LL‑37 can stick to the hormone IAPP, which normally clumps together in the pancreas and harms insulin‑producing cells in type‑2 diabetes. In lab tests, LL‑37 stopped these clumps from forming and protected the cells, suggesting it might help guard against diabetes‑related damage.
Hemshekhar. Mahadevappa M; Faiyaz. Sana S; Choi. Ka-Yee Grace KG; Krokhin. Oleg V OV; Mookherjee. Ne...
The study shows that tiny changes in the shape and water‑loving nature of LL‑37‑derived peptides dramatically affect how well they calm down inflammation caused by bacterial toxins. Even though all the tested peptides have the same positive charge, only those that are more helical and hydrophobic can strongly block inflammatory signals in immune cells.
Fabisiak. Natalia N; Fabisiak. Adam A; Chmielowiec-Korzeniowska. Anna A; Tymczyna. Leszek L; Kamysz....
A short piece of the human immune peptide LL-37, called KR-12, was given to mice with chemically‑induced gut inflammation. The treatment lowered gut damage scores, reduced inflammation markers, and cut down harmful bacteria in the stool, suggesting it might help with inflammatory bowel disease—but only in animal models so far.
Inomata. Megumi M; Horie. Toshi T; Into. Takeshi T
The study shows that the natural antimicrobial peptide LL‑37 can change how gum cells react to bacterial toxins. At low doses it isn’t toxic, but it can both boost and calm down inflammation depending on whether the cells are already exposed to bacterial LPS. It does this by acting on a receptor called P2X7 and by tweaking several immune‑related genes.
Human proteins like LL‑37, which our bodies naturally make, can fight many kinds of viruses by breaking their outer layers and stopping infection steps. Scientists have seen this effect in lab dishes and animal studies, and they think these proteins could become new antiviral drugs, but we don’t yet know how to safely use them on our own.
The study shows that the human antimicrobial peptide LL-37 can grab onto hidden iron‑stealing molecules (stealth siderophores) that some bacteria use to become more dangerous. When LL-37 binds these molecules, it folds into a more active shape, and the attraction is mainly due to electric charges. This suggests LL-37 helps the immune system mop up bacterial iron‑chelation tools, adding another layer to how our bodies fight infection.
Zhu. Chuanan C; Zhou. Yingfan Y; Zhu. Jiabin J; Liu. Ye Y; Sun. Mengyi M
In people with community‑acquired pneumonia, those who are sicker have higher blood levels of the inflammation protein NLRP3 and lower levels of the antimicrobial peptide LL‑37. The combination of high NLRP3 and low LL‑37 predicts a worse chance of surviving 30 days.
Zhang. Zhifang Z; Le. Keith K; La Placa. Deirdre D; Armstrong. Brian B; Miller. Marcia M MM; Shively...
The study shows that the immune‑boosting peptide LL‑37 is taken up by human monocytes and stays inside the cells for days, helping them turn into a special bone‑repair cell called a monoosteophil. This process involves the CXCR2 receptor and several cellular pathways, and the peptide ends up in large, stable vesicles that also contain other surface proteins.
Patiño Vargas. Maria Isabel MI; Mesa Cadavid. Mónica M; Arenas Gómez. Claudia Marcela...
Scientists made tiny particles (polyplexes) that can carry DNA into skin cells without using viruses. When they used a linear form of a polymer called PEI, the skin cells made more of the natural antibiotic peptide LL‑37 and the liquid from those cells could kill Staphylococcus aureus in a lab test. The branched form of the polymer was more toxic to the cells.
Kamysz. Elżbieta E; Sikorska. Emilia E; Jaśkiewicz. Maciej M; Bauer. Marta M; Neubauer....
Scientists added different fatty‑acid tails to a short piece of the natural antimicrobial peptide LL‑37 (called KR12). Adding a medium‑length tail (about 8 carbons) made the peptide kill drug‑resistant bacteria at low doses, but longer tails (like 14 carbons) caused the peptide to clump together and become less effective. All the fatty‑acid‑modified versions were also more toxic to human cells, meaning safety is a big concern.
The study found that the antimicrobial peptide LL‑37, together with bacterial LPS, makes old (senescent) blood‑vessel cells more inflammatory by boosting a molecule called ICAM‑1 and turning on the NF‑κB pathway. This heightened inflammation could help drive atherosclerosis, especially in older people whose blood‑vessel cells are already senescent.
The study shows that the antimicrobial peptide LL‑37 helps immune cells (macrophages) eat up DNA webs (NETs) that are left behind after neutrophils trap microbes. Without LL‑37, these DNA webs aren’t taken up well, but adding the peptide restores the process. NETs themselves don’t cause inflammation, but they can change how cells react to bacterial signals.
The study shows that a bacterial enzyme (ApdS) from Streptococcus suis can cut up the human antimicrobial peptide LL‑37, making it less able to kill the bacteria and to activate immune cells. When the bacteria encounter LL‑37, they produce more of this enzyme, which helps them evade the body's first line of defense.
John. Constance M CM; Li. Min M; Feng. Dongxiao D; Jarvis. Gary A GA
A short, positively‑charged peptide can kill the bacteria that cause gonorrhea in lab tests, gets inside the bacteria, and stops them from invading human cells or triggering inflammation, while not harming human immune cells. However, this work is still early‑stage and done only in cell cultures, so it isn’t ready for personal use yet.
Damour. Alexia A; Garcia. Magali M; Seneschal. Julien J; Lévêque. Nicolas N; Bodet. Charle...
The review explains why people with eczema (atopic dermatitis) are more likely to get a serious herpes skin infection called eczema herpeticum. One key reason is that their skin makes less of the natural antimicrobial peptide LL‑37, which normally helps fight microbes and viruses. Other factors include skin barrier problems, immune signaling changes, and bacterial overgrowth.
Honda. Jennifer R JR; Hess. Tamara T; Carlson. Rachel R; Kandasamy. Pitchaimani P; Nieto Ramirez. Lu...
The study shows that different types of non‑TB mycobacteria infect immune cells to varying degrees, and some of them can protect themselves from the natural antibacterial peptide LL‑37 by using special fats in their cell walls.
Khan. Ayesha A; Davlieva. Milya M; Panesso. Diana D; Rincon. Sandra S; Miller. William R WR; Diaz. L...
The study shows that the human antimicrobial peptide LL‑37 is recognized by a bacterial protein called LiaX in Enterococcus faecalis. When LL‑37 (or the antibiotic daptomycin) binds to LiaX, the bacteria remodel their cell membrane to push the drug away, making them more resistant and even more virulent in a worm infection model.