An antimicrobial peptide of the cathelicidin family that provides innate immune defense by killing pathogens and modulating inflammation and wound healing.
Gable. Jonathan E JE; Schlamadinger. Diana E DE; Cogen. Anna L AL; Gallo. Richard L RL; Kim. Judy E...
This study shows that two engineered versions of the human antimicrobial peptide LL‑37 work just as well as the natural peptide at killing bacteria and breaking cell membranes. Using special light‑based techniques, the researchers found that the tryptophan tags they added behave similarly in water, carbonate solutions, and when the peptide interacts with lipid membranes, supporting a membrane‑disruption mode of action.
Barlow. Peter G PG; Beaumont. Paula E PE; Cosseau. Celine C; Mackellar. Annie A; Wilkinson. Thomas S...
The study shows that the natural protein LL‑37, which our bodies make in the lungs, helps kill airway cells that are infected with the bacteria Pseudomonas aeruginosa. It does this by triggering a controlled cell‑death process (apoptosis) only when both the peptide and live bacteria are present, using the cell’s mitochondria and caspase enzymes. High, non‑physiological levels of LL‑37 cause a different, uncontrolled cell death.
Jiang. Ziqing Z; Higgins. Michael P MP; Whitehurst. James J; Kisich. Kevin O KO; Voskuil. Martin I M...
Researchers tested specially designed short proteins (peptides) against regular and drug‑resistant TB bacteria. The D‑form peptide called D5 stopped bacterial growth at low concentrations, and a similar peptide D1 worked almost as well but was less harmful to human cells. The natural human peptide LL‑37 didn’t do much against TB.
Tecle. Tesfaldet T; Tripathi. Shweta S; Hartshorn. Kevan L KL
Defensins and the peptide LL‑37 are natural proteins made by immune cells and airway lining cells that kill germs and help control inflammation in the lungs. This review explains the different types of defensins, their broad antimicrobial actions, and how they also recruit immune cells and can calm inflammation. It notes that LL‑37 works similarly, but we still need to figure out exactly how much each contributes to lung health.
Fazliana. Mansor M; Ramos. Nubia L NL; Lüthje. Petra P; Sekikubo. Musa M; Holm. Asa A; Wan Naza...
A Malaysian herb called Labisia pumila var. alata (LPva) can make bladder cells die in a controlled way, which helps lower the number of urinary‑tract bacteria that hide inside those cells. It doesn't kill the bacteria directly and doesn't change levels of the natural antimicrobial peptide LL‑37, but by prompting the infected cells to undergo apoptosis it reduces bacterial invasion.
Bell. S S; Howard. A A; Wilson. J A JA; Abbot. E L EL; Smith. W D WD; Townes. C L CL; Hirst. B H BH;...
The study looked at how the natural antimicrobial peptides LL‑37 (hCAP‑18) and beta‑defensins behave in tonsils during a strep throat infection. It found that, when the infection is active, the tonsil cells make less LL‑37 and defensins, especially in people who get frequent tonsillitis, suggesting these peptides help protect the throat but are suppressed during infection.
Researchers found that the natural peptide LL‑37, which is released by neutrophils, helps blood vessels heal faster after a stent is placed, cutting down the thickening that can block the artery again. In mice, a tiny stent coated with LL‑37 reduced this re‑narrowing, showing the peptide’s potential to improve vascular recovery.
Pasupuleti. Mukesh M; Roupe. Markus M; Rydengård. Victoria V; Surewicz. Krystyna K; Surewicz. W...
Researchers found that the front part of the human prion protein can kill bacteria and fungi, acting much like the well‑known antimicrobial peptide LL‑37 by punching holes in cell membranes. Unlike LL‑37, these prion‑derived pieces don’t form a helix when they hit bacterial membranes, and the protein’s levels go up when skin is wounded, hinting it helps protect wounds.
Mader. Jamie S JS; Ewen. Catherine C; Hancock. Robert E W RE; Bleackley. Robert C RC
The human antimicrobial peptide LL-37 can kill regulatory T cells (the immune cells that calm down immune responses) at much lower doses than it harms other immune cells. It does this by triggering apoptosis through enzymes called granzymes, and the effect can be both caspase‑dependent and independent. This suggests LL-37 might be used to dampen the suppressive immune environment around tumors.
Pence. Morgan A MA; Rooijakkers. Suzan H M SH; Cogen. Anna L AL; Cole. Jason N JN; Hollands. Andrew...
The study shows that a protein made by dangerous strep bacteria (SIC) can grab and neutralize the human antimicrobial peptide LL‑37, helping the bacteria survive in blood and cause infection. This means LL‑37’s natural defense role can be blocked by certain bacterial strains.
Scientists figured out a way to grow a lot more early endothelial progenitor cells (EPCs) from umbilical cord blood in the lab. During this process the gene for the peptide LL‑37 (CAMP) became the most strongly increased, along with other genes linked to heart protection and new blood‑vessel growth.
Brandenburg. Lars-Ove LO; Jansen. Sandra S; Wruck. Christoph J CJ; Lucius. Ralph R; Pufe. Thomas T
The study shows that the antimicrobial peptide LL‑37 (called rCRAMP in rats) can activate brain support cells called glia, causing them to release inflammation signals and growth factors, and this effect works through a specific brain receptor (P2Y11).
The study shows that a protein called APE1 controls inflammation in skin cells and also boosts the production of the antimicrobial peptide LL‑37. In psoriasis, APE1 levels are higher, and it helps activate key inflammation pathways. While this reveals a new link, it doesn’t give a clear way to use LL‑37 or APE1 in everyday health hacks yet.
Pathan. Firoz K FK; Venkata. Deepa A DA; Panguluri. Siva K SK
This paper reviews recent patents on antimicrobial peptides, highlighting that scientists are trying to turn these natural antibiotics into new medicines. It mentions that the human peptide LL‑37 and its modified versions are being patented for helping wounds heal, but it doesn’t give any dosing or how‑to‑use details. The focus is on the patent landscape rather than new experimental results you could try right now.
Rupec. Rudolf A RA; Boneberger. Susanne S; Ruzicka. Thomas T
The abstract says that eczema (atopic dermatitis) is linked to genetics, skin barrier problems, and a messed‑up immune response, and that the skin’s natural antimicrobial peptide LL‑37 is lower in affected people. It doesn’t give a new treatment, just points out that LL‑37 and other defenses are part of the disease puzzle.
Neville. Frances F; Ivankin. Andrey A; Konovalov. Oleg O; Gidalevitz. David D
The study shows that the human peptide LL‑37 and the animal peptide SMAP‑29 both target negatively charged cell membranes, but SMAP‑29 needs a lot more molecules to break the membrane even though it’s more positively charged. This means that a peptide’s shape and size matter as much as its charge when it interacts with membranes.
Brandenburg. Lars-Ove LO; Varoga. Deike D; Nicolaeva. Nicoletta N; Leib. Stephen L SL; Podschun. Rai...
The study shows that brain‑covering cells in rats make the antimicrobial peptide LL‑37’s counterpart (rCRAMP) when they sense bacterial signals, and this peptide can kill bacteria in lab tests. It also shows that inflammation signals boost its production, and that the peptide shows up in infected rat brains. However, the work is basic science in rats and doesn’t give dosage or safety info for humans.
This paper reviews how natural antimicrobial peptides like LL‑37 act as the body’s first line of defense in skin and gut, killing microbes and shaping immune responses. It notes that LL‑37 levels rise in psoriasis but drop in eczema, linking these peptides to inflammation and disease states, but it doesn’t give any dosing or treatment tips.
The paper explains how certain immune sensors (TLR3,7,8,9) spot DNA and RNA inside cells, and how the natural peptide LL‑37 can bind these nucleic acids and help trigger those sensors. While this shows LL‑37’s role in immune activation, it doesn’t give any direct dosing tips or protocols for everyday use.
van der Weerden. Nicole L NL; Hancock. Robert E W RE; Anderson. Marilyn A MA
This study looked at how a plant protein called NaD1 kills fungus and compared it to other antimicrobial peptides, including the human peptide LL‑37. It found that NaD1 needs the fungus’s cell wall to work, while LL‑37 is thought to act mainly by breaking cell membranes, but the paper didn’t reveal any new tricks for using LL‑37 in humans.