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LL-37

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.

Quick Stats
Studies 2230
Trials 95
Formula C205H340N60O53
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Utility 2
pubmed Oct 23, 2021

Evaluation of LL-37 in healing of hard-to-heal venous leg ulcers: A multicentric prospective randomized placebo-controlled clinical trial.

Mahlapuu. Margit M; Sidorowicz. Adam A; Mikosinski. Jacek J; Krzyżanowski. Mikołaj M; Or...

A phase IIb trial tested a skin cream containing the peptide LL-37 on tough venous leg ulcers. Overall it didn’t heal ulcers faster than a placebo, but in a side analysis people with big wounds (≥10 cm²) seemed to heal better. The cream was safe at both tested doses.

Utility 2
pubmed Jan 1, 2021

IL-27 induces LL-37/CRAMP expression from intestinal epithelial cells: implications for immunotherapy of <i>Clostridioides difficile</i> infection.

Xu. Banglao B; Wu. Xianan X; Gong. Yi Y; Cao. Ju J

The study shows that the immune signal IL‑27 can boost the body’s natural antimicrobial peptide LL‑37 in gut cells, helping clear C. difficile infections in mice and linking higher IL‑27 and LL‑37 levels in infected patients. While it highlights a promising immune pathway, it doesn’t give a ready‑to‑use supplement or protocol for everyday use.

Utility 2
pubmed Apr 6, 2022

Human Cathelicidin Peptide LL-37 Induces Cell Death in Autophagy-Dysfunctional Endothelial Cells.

Suzuki. Kaori K; Ohkuma. Mari M; Someya. Akimasa A; Mita. Tomoya T; Nagaoka. Isao I

The study shows that the natural antimicrobial peptide LL‑37 can start the cell’s recycling process (autophagy) in blood‑vessel cells, but if the recycling system is broken, LL‑37 builds up and kills those cells, which might help explain plaque formation in arteries.

Utility 2
pubmed Dec 20, 2021

The antimicrobial peptide LL-37 triggers release of apoptosis-inducing factor and shows direct effects on mitochondria.

Bankell. Elisabeth E; Liu. Xiaoyan X; Lundqvist. Martin M; Svensson. Daniel D; Sw&#xe4;rd. Karl K; S...

The study shows that the human peptide LL‑37 quickly gets inside bone‑like cells and gathers in the mitochondria, where it makes the cells release proteins that trigger cell death. It also directly makes the mitochondrial membrane leaky. This means LL‑37 can damage healthy cells by messing with their power plants, which is important to know before anyone tries to use it as a supplement or therapy.

Utility 2
pubmed Dec 1, 2021

High Human Antimicrobial Peptide LL-37 Level Predicts Lower Major Adverse Cardiovascular Events after an Acute ST-Segment Elevation Myocardial Infarction.

Zhao. Hanjun H; Sheng. Zhaoxue Z; Tan. Yu Y; Chen. Runzhen R; Zhou. Jinying J; Li. Jiannan J; Zhao....

People who have higher natural levels of the antimicrobial peptide LL‑37 in their blood after a heart attack tend to have fewer serious heart problems over the next three years, while those with lower levels have more complications and higher death rates.

Utility 2
pubmed Oct 3, 2021

Antimicrobial Peptide, LL-37, And Its Potential As An Anti-HIV Agent.

Vera-Cruz. Ana A; Tanphaichitr. Nongnuj N; Angel. Jonathan B JB

LL-37 is a natural antimicrobial peptide that shows some ability to block HIV infection in lab tests and may also affect the virus’s enzymes, but the evidence is still early and mixed. It also kills other sexually‑transmitted germs and can act as a sperm blocker, so it could become a multi‑purpose gel or spray for sexual health, though more research is needed before anyone can use it safely.

Utility 2
pubmed Sep 23, 2021

Cathelicidin LL-37 Ignites Primed NLRP3 Inflammasomes in Rosacea.

Croitoru. David O DO; Piguet. Vincent V

The study shows that the skin peptide LL‑37, which rises after UV light, infections or injury, can trigger a strong inflammatory response in rosacea by activating a cellular alarm called the NLRP3 inflammasome. In mouse skin, injecting LL‑37 caused redness and swelling, but blocking NLRP3 stopped the reaction.

Utility 2
pubmed Feb 21, 2022

The long-term prognostic value of serum 25(OH)D, albumin, and LL-37 levels in acute respiratory diseases among older adults.

Aronen. Matti M; Viikari. Laura L; Langen. Henriikka H; Kohonen. Ia I; Wuorela. Maarit M; Vuorinen....

In older adults hospitalized for breathing problems, low blood albumin (a protein that reflects nutrition and overall health) predicts higher short‑ and long‑term death risk, while vitamin D and the antimicrobial peptide LL‑37 don’t seem to affect disease severity or survival.

Utility 2
pubmed Feb 26, 2022

The human LL-37 peptide exerts antimicrobial activity against Legionella micdadei interacting with membrane phospholipids.

Palusi&#x144;ska-Szysz. Marta M; Jurak. Ma&#x142;gorzata M; Gisch. Nicolas N; Waldow. Franziska F; Z...

The study shows that the human antimicrobial peptide LL‑37 can kill the pneumonia‑causing bacteria Legionella micdadei, and that when the bacteria are grown with extra choline (a nutrient found in many foods), they become even more sensitive to LL‑37 because their membrane changes. This reveals a link between bacterial membrane makeup and how well our natural defenses work, but it doesn’t give a ready‑to‑use supplement or treatment plan for most people.

Utility 2
pubmed Oct 11, 2021

Quorum Sensing <i>Pseudomonas</i> Quinolone Signal Forms Chiral Supramolecular Assemblies With the Host Defense Peptide LL-37.

Zsila. Ferenc F; Ricci. Maria M; Szigy&#xe1;rt&#xf3;. Imola Csilla IC; Singh. Priyanka P; Beke-Somfa...

Scientists found that the human antimicrobial peptide LL‑37 can grab onto a signaling molecule used by Pseudomonas bacteria, forming tiny twisted structures that lock the signal inside. This may stop the bacteria from talking to each other and forming tough biofilms, offering a new way the peptide could fight infections.

Utility 2
pubmed Dec 22, 2021

Utilizing the Potential of Antimicrobial Peptide LL-37 for Combating SARS-COV- 2 Viral Load in Saliva: an In Silico Analysis.

Nireeksha. Nireeksha N; Gollapalli. Pavan P; Varma. Sudhir Rama SR; Hegde. Mithra N MN; Kumari. N Su...

The study used computer models to see if the natural antimicrobial peptide LL‑37 could break apart the COVID‑19 virus in saliva. The simulations suggest LL‑37 might stick to and disrupt the virus’s outer membrane, potentially working against all known variants, but no lab or human tests were done yet.

Utility 2
pubmed Dec 9, 2022

HBD-2 variants and SARS-CoV-2: New insights into inter-individual susceptibility.

Behairy. Mohammed Y MY; Soltan. Mohamed A MA; Eldeen. Muhammad Alaa MA; Abdulhakim. Jawaher A JA; Al...

Researchers used computer models to find three genetic changes (SNPs) in the natural antimicrobial peptide hBD‑2 that make the protein less stable and weaker at sticking to the COVID‑19 virus spike protein. These changes could make some people more vulnerable to infection, and the findings could help develop personalized risk‑assessment tools.

Utility 2
pubmed Jan 17, 2022

Cathelicidin hCAP18/LL-37 promotes cell proliferation and suppresses antitumor activity of 1,25(OH)<sub>2</sub>D<sub>3</sub> in hepatocellular carcinoma.

Zhang. Huidan H; Zhen. Junai J; Zhang. Rong R; Wanyan. Yangke Y; Liu. Kehang K; Yuan. Xueli X; Tao....

The peptide LL‑37, which helps fight infections, was found to make liver cancer cells grow faster and to block the anti‑cancer effects of vitamin D in lab dishes and mouse tumors. It does this by turning on the EGFR/HER2‑Akt signaling pathway. Vitamin D itself raises LL‑37 levels, which could unintentionally reduce vitamin D’s own tumor‑fighting power in liver cancer.

Utility 2
pubmed Nov 9, 2022

Human cathelicidin LL-37 exerts amelioration effects against EHEC O157:H7 infection regarding inflammation, enteric dysbacteriosis, and impairment of gut barrier function.

Fang. Xin X; Nong. Keyi K; Wang. Zihan Z; Jin. Yuanli Y; Gao. Feng F; Zeng. Qiuyu Q; Wang. Xuemei X;...

In mice infected with a harmful E. coli strain, giving the natural peptide LL‑37 helped keep weight stable, protected gut lining, lowered inflammation, and improved the balance of gut bacteria. It also reduced the spread of bacteria to the liver and kidneys, suggesting LL‑37 can boost gut health during infection.

Utility 2
pubmed Oct 13, 2021

Proteinous Components of Neutrophil Extracellular Traps Are Arrested by the Cell Wall Proteins of <i>Candida albicans</i> during Fungal Infection, and Can Be Used in the Host Invasion.

Karkowska-Kuleta. Justyna J; Smolarz. Magdalena M; Seweryn-Ozog. Karolina K; Satala. Dorota D; Zawro...

The study shows that a natural immune peptide called LL‑37, which is part of neutrophil traps, sticks to the surface of the fungus Candida albicans. When the fungus grabs LL‑37 and other trap proteins, it actually becomes better at damaging human cells, suggesting the fungus can hijack these immune molecules.

Utility 2
pubmed Aug 7, 2021

HD5 and LL-37 Inhibit SARS-CoV and SARS-CoV-2 Binding to Human ACE2 by Molecular Simulation.

Li. Daixi D; Chen. Peiqin P; Shi. Ting T; Mehmood. Aamir A; Qiu. Jingfei J

A computer‑model study found that the natural peptide LL‑37 sticks to the part of the ACE2 protein that the coronavirus uses to get into cells, even better than another peptide called HD5. This suggests LL‑37 might be able to block the virus from attaching, but the work is only theoretical and hasn’t been tested in people yet.

Utility 2
pubmed Nov 25, 2021

Human Antimicrobial Peptide Triggered Colloidal Transformations in Bacteria Membrane Lipopolysaccharides.

Hong. Linda L; Gontsarik. Mark M; Amenitsch. Heinz H; Salentinig. Stefan S

Researchers studied how the human antimicrobial peptide LL‑37 interacts with the outer membrane layer (LPS) of E. coli and how it behaves when packed inside tiny lipid particles. They found that LL‑37 can change LPS structures and that putting LL‑37 into special lipid carriers alters these changes, which could help design better antibacterial nanomaterials.

Utility 2
pubmed Jan 6, 2022

Molecular Mechanisms of <i>Staphylococcus</i> and <i>Pseudomonas</i> Interactions in Cystic Fibrosis.

Biswas. Lalitha L; G&#xf6;tz. Friedrich F

This review explains how two common lung bacteria in cystic fibrosis, Staphylococcus aureus and Pseudomonas aeruginosa, fight and help each other, and why the human antimicrobial peptide LL‑37 often can’t kill them. S. aureus can change into a tiny, slow‑growing form that resists antibiotics and LL‑37, while P. aeruginosa releases toxins that suppress S. aureus but also adapts its own defenses. The bacteria even protect each other from immune cells, making infections harder to clear.

Utility 2
pubmed Oct 26, 2021

Cardiolipin prevents pore formation in phosphatidylglycerol bacterial membrane models.

Rocha-Roa. Cristian C; Orjuela. Juan David JD; Leidy. Chad C; Cossio. Pilar P; Aponte-Santamar&#xed;...

The study shows that a bacterial membrane fat called cardiolipin makes it harder for the antimicrobial peptide LL‑37 to punch holes in the membrane, helping bacteria like Staph aureus resist the peptide. This was seen in computer simulations, not in real people or animals.