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Cathelicidin, hCAP-18, FALL-39, CAP-18
An antimicrobial peptide of the cathelicidin family that provides innate immune defense by killing pathogens and modulating inflammation and wound healing.
Malmsten. Martin M; Davoudi. Mina M; Walse. Björn B; Rydengård. Victoria V; Pasupuleti. Mu...
Scientists found that short pieces taken from several growth‑factor proteins can kill bacteria and fungi, working like the natural antimicrobial peptide LL‑37 by breaking cell membranes, and they don’t damage red blood cells.
Mookherjee. Neeloffer N; Wilson. Heather L HL; Doria. Silvana S; Popowych. Yurij Y; Falsafi. Reza R;...
The study shows that the natural peptide LL‑37 (and its cow version BMAP‑27) can strongly dampen the inflammatory response that cells have to bacterial toxins, even at low doses that could be reached in the body. This anti‑inflammatory effect works by blocking the activation of NF‑κB, a key driver of inflammation.
von Köckritz-Blickwede. Maren M; Goldmann. Oliver O; Thulin. Pontus P; Heinemann. Katja K; Norr...
Mast cells can trap and kill bacteria using web‑like structures called MCETs, and these webs contain the antimicrobial peptide LL‑37, showing another way the body uses LL‑37 to fight infection.
Frick. Inga-Maria IM; Akesson. Per P; Herwald. Heiko H; Mörgelin. Matthias M; Malmsten. Martin...
The study shows that when the body’s contact system is activated, it creates a short 26‑amino‑acid piece that can kill bacteria just as well as the well‑known antimicrobial peptide LL‑37, even in normal salt conditions. Blocking this system in mice makes infections spread faster, highlighting its protective role.
Chromek. Milan M; Slamová. Zuzana Z; Bergman. Peter P; Kovács. László L; Podrack...
The body makes a natural antimicrobial peptide called LL‑37 in the lining of the bladder and urethra. When bacteria touch these cells, LL‑37 is quickly released into urine and helps kill the germs. Mice that can’t make this peptide get more urinary infections, and human‑derived bacteria that are resistant to LL‑37 cause worse infections.
Mak. Pawel P; Siwek. Michal M; Pohl. Jan J; Dubin. Adam A
Researchers found that a small protein piece from hemoglobin, called HbB115-146, kills bacteria especially well in the acidic environment of the vagina and works even when salt is present. It also boosts the power of other natural antimicrobial proteins like LL‑37, HNP‑1, and lysozyme, especially at low pH.
Gaudreault. Eric E; Gosselin. Jean J
The study shows that a natural inflammation molecule, leukotriene B4 (LTB4), can trigger immune cells to release antiviral peptides like LL‑37, cutting down cytomegalovirus (CMV) levels in lab tests. This effect needs the BLT1 receptor and active neutrophils, and blocking the released peptides weakens the antiviral action.
Jeng. Leo L; Yamshchikov. Alexandra V AV; Judd. Suzanne E SE; Blumberg. Henry M HM; Martin. Gregory...
The study found that people in the ICU with sepsis have lower vitamin D and lower levels of the natural antimicrobial peptide LL‑37, and that higher vitamin D levels are linked to higher LL‑37. This suggests that keeping vitamin D sufficient might help the body’s innate immune defenses, especially during severe infections.
Martineau. Adrian R AR; Newton. Sandra M SM; Wilkinson. Katalin A KA; Kampmann. Beate B; Hall. Bridg...
The study shows that the natural antimicrobial peptide LL-37, made by neutrophils, helps stop the growth of TB bacteria, and having more neutrophils or higher LL-37 levels is linked to lower TB infection risk. This suggests that boosting LL-37 could be a strategy for better innate defense against TB, though the research doesn’t give a direct supplement plan.
Aberg. Karin M KM; Man. Mao-Qiang MQ; Gallo. Richard L RL; Ganz. Tomas T; Crumrine. Debra D; Brown....
The study shows that the skin’s natural antimicrobial peptide LL‑37 (called CRAMP in mice) rises when the skin barrier is damaged and helps the barrier heal back, while blocking barrier repair stops this peptide’s increase. Mice missing LL‑37 recover more slowly, proving the peptide is important for skin health.
Ball. S L SL; Siou. G P GP; Wilson. J A JA; Howard. A A; Hirst. B H BH; Hall. J J
The study found that human tonsils naturally produce several antimicrobial peptides, including LL‑37, which help defend against infections. People with recurrent tonsillitis had lower levels of LL‑37 and some other peptides on the surface of their tonsils, which might make them more prone to infections.
Chakraborty. Krishnendu K; Ghosh. Shubhamoy S; Koley. Hemanta H; Mukhopadhyay. Asish Kumar AK; Ramam...
The study shows that harmful gut bacteria, especially cholera and certain E. coli strains, release toxins that shut down the production of two important natural antibiotics in our intestinal lining, LL-37 and HBD-1. These toxins work by hijacking cell signaling pathways that involve cAMP, PKA, and other proteins, leading to less of these protective peptides.
Sevcsik. E E; Pabst. G G; Jilek. A A; Lohner. K K
LL-37, a natural human peptide, breaks cell membranes in two different ways depending on the type of fats in the membrane: it creates a special interlocked structure in membranes with negatively charged lipids, and it breaks apart neutral membranes into tiny micelles. The way it works changes with the length of the fatty‑acid chains and how much peptide is present. This means the peptide’s effect can vary a lot depending on the lipid makeup of the target cells or any delivery vehicle you use.
Martineau. Adrian R AR; Wilkinson. Katalin A KA; Newton. Sandra M SM; Floto. R Andres RA; Norman. An...
The study shows that the active form of vitamin D can boost the body's own antimicrobial peptide, LL-37, which in turn can dramatically cut the growth of the TB bacteria in lab tests. Vitamin D does this without relying on the usual immune signals like IFN‑gamma or TNF, pointing to a different way the vitamin helps fight infection.
Sood. Rohit R; Domanov. Yegor Y; Pietiäinen. Milla M; Kontinen. Vesa P VP; Kinnunen. Paavo K J...
The study shows that the human antimicrobial peptide LL‑37 sticks strongly to cell membranes that contain acidic fats (like many bacteria) but is blocked by membranes rich in cholesterol and sphingomyelin (like our own cells). This explains why LL‑37 can kill microbes without hurting us at normal levels, but high doses can still damage cells.
Wang. Guangshun G; Watson. Karen M KM; Buckheit. Robert W RW
Scientists tested short pieces of the natural protein LL‑37 and a similar bovine protein to see if they can block HIV. They found that a tiny fragment called FK‑13 can stop the virus, while another fragment, GI‑20, works best with the fewest side effects. A bovine‑derived peptide, BMAP‑18, performed about as well as GI‑20. The shape and certain amino acids of these peptides are key to their antiviral action.
Schwab. Markus M; Reynders. Veerle V; Shastri. Yogesh Y; Loitsch. Stefan S; Stein. Jürgen J; Sc...
Scientists found that the short‑chain fatty acid butyrate, which your gut makes from fiber, can boost the production of the natural antibiotic LL‑37 in colon cells. This boost relies on the vitamin D receptor and certain cell‑signaling pathways, but not on the PPAR‑gamma pathway.
Gordon. Y Jerold YJ; Huang. Ling C LC; Romanowski. Eric G EG; Yates. Kathleen A KA; Proske. Rita J R...
The study shows that the natural peptide LL‑37 is made by eye surface cells and can kill common eye‑infecting bacteria and viruses at low concentrations without harming human lung cells, suggesting it could be a safe, broad‑spectrum antimicrobial for the eye.
Zelezetsky. Igor I; Pontillo. Alessandra A; Puzzi. Luca L; Antcheva. Nikolinka N; Segat. Ludovica L;...
The study shows that the antimicrobial peptide LL‑37 has evolved different versions in primates. Some versions (like those from macaques) stay unstructured in solution and kill microbes strongly regardless of salt levels, while the human version and a few others need salt to fold and work, and they interact differently with our own cells. This means the way LL‑37 works can change a lot depending on its exact shape and the surrounding environment.
Lee. Hye-Mi HM; Shin. Dong-Min DM; Choi. Dae-Kyoung DK; Lee. Zee-Won ZW; Kim. Ki-Hye KH; Yuk. Jae-Mi...
The study shows that skin cells (keratinocytes) use the antimicrobial peptide LL‑37 to fight the bacteria that cause Buruli ulcer. When the cells detect the bacteria through specific receptors (TLR2, TLR4, Dectin‑1), they produce reactive oxygen species (ROS) which trigger more LL‑37, helping to keep the infection in check. Blocking ROS or LL‑37 lets the bacteria grow more, highlighting LL‑37’s protective role.