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(630) 426-1472
info@corepeptidesbuyusa.com
5401 S Kirkman Rd suite 310, Orlando FL 32819
$79.00
LL-37 peptide, also known as Cathelicidin, is a 37-amino-acid cationic peptide widely studied for its potential role in antimicrobial defense, immune response, inflammatory signaling, and tissue repair. Popular in advanced laboratory research, LL-37 is valued for its relevance in studies involving microbial membrane interaction, innate immunity, wound healing, and host defense mechanisms. For research and laboratory use only.
Size: 5mg
Contents: LL-37 (5mg)
Form: Lyophilized powder
Purity: >99%
SKU: P-LL37-5
LL-37, also known as Cathelicidin, is a cationic peptide composed of 37 amino acids and is primarily found in neutrophils.(1) The peptide is believed to be produced through the extracellular breakdown of hCAP18 proteins by protease enzymes. In research settings, LL-37 is widely studied for its potential antimicrobial properties. It has also been suggested that the peptide may form agglomerates and lipid bilayers, which could help protect it from degradation and enzymatic action.(1)
Antimicrobial peptides are structured compounds researched for their potential activity against bacteria, fungi, and certain virus strains. These peptides may interact with their targets in a non-specific manner, which has led researchers to suggest that pathogens may be less likely to develop resistance against them.(2)
LL-37 is an α-helical peptide that scientists believe may play an important role in maintaining defense against microbes.(3) To better understand its activity, a peptide model was developed in one study(4) based on the theory that LL-37 may interact directly with bacterial membranes. According to this work, the peptide may first bind to membrane lipids through electrostatic interactions, followed by lateral diffusion and assembly on the membrane surface. This interaction may then contribute to membrane disruption and possible degradation of the bacterial cell.
Several additional studies have proposed other possible mechanisms for LL-37 interaction with microbial membranes, including pore formation on the membrane(3)(5) and extensive membrane disruption caused by peptide-lipid complexes.(6) Together, these findings support the view that LL-37 may exert biological effects through direct interaction with microbial membranes. You may also be interested in our related research peptides, including Tripeptide, Sermorelin Peptide, Hexarelin, Melanotan 1, Oxytocin Peptide, Snap 8 Peptide, Pinealon, Kisspeptin 10 mg, VIP Peptide, and ARA 290 Peptide.
Molecular Formula: C205H340N50O53
Molecular Weight: 4493.34 g/mol
Other Known Titles: CAP-18
The main goal of this study(7) was to evaluate the inflammatory potential of LL-37. Tissue cultures were used, with one group left unaltered and another exposed to U1 RNA, a non-coding RNA released during tissue injury. LL-37 peptide was then added to both cultures. Based on genetic analysis, researchers suggested that the culture treated with both U1 RNA and LL-37 peptide produced a significant response related to epidermal inflammation and defense mechanisms.
The study proposed that LL-37 might enhance immune responses to damaged cells by influencing how self-nucleic acids such as DNA and RNA are recognized. This recognition may occur when LL-37 interacts with specific cellular receptors, including scavenger receptors (SRs), potentially leading to clathrin-dependent endocytosis. This process appears important for the later activation of inflammatory pathways inside the cells. The same study also suggested that LL-37 may support the binding of dsRNA to scavenger receptors, which may then trigger signaling events that lead to cytokine expression. In particular, the interaction between LL-37 and scavenger receptors such as SR-A6 and SR-B1 may be significant, as blocking these receptors with a competitive inhibitor like fucoidan or silencing their expression appeared to reduce cytokine production.
Another notable finding from this study is the suggestion that LL-37 may modulate immune responses by influencing intracellular signaling pathways, including Toll-like receptors (TLR) and interferon regulatory factors, which may be activated in response to foreign nucleic acids. As described in the study, clathrin-mediated endocytosis may help enable the entry of immune-modulating molecules into cells, an important step in triggering immune activity.
The primary aim of this study(1) was to better understand the role of LL-37 in autoimmune models such as psoriasis. The researchers suggested that endogenous LL-37 may form complexes with DNA, potentially increasing interferon-related activity and inflammatory responses. The study also theorized that LL-37 may be beneficial in tissue and wound injury, while elevated peptide levels may also be linked with psoriasis. In addition, LL-37 may exert anti-apoptotic actions on keratinocytes, which could contribute to the cellular proliferation observed in psoriatic lesions. As a naturally occurring antimicrobial peptide, LL-37 forms part of the innate immune system and appears to play several roles in immune regulation. This activity may contribute to the development of the thick, scaly skin commonly associated with psoriasis.
Although LL-37 has been implicated in promoting inflammation through type I interferon pathways, it also appears to provide a protective effect against activation of the AIM2 inflammasome by cytosolic double-stranded DNA (dsDNA). Cytosolic dsDNA often triggers immune responses that may lead to inflammation. In situations where LL-37 forms complexes with DNA, these complexes seem not to promote interleukin-1β (IL-1β) production or inflammasome activation. This suggests that LL-37 may help protect keratinocytes from inflammatory responses typically triggered by the AIM2 inflammasome in the presence of dsDNA. This dual activity highlights the complex role of LL-37 in immune regulation and inflammatory signaling.
The main objective of these studies(1)(8) was to evaluate the possible role of LL-37 in arthritic joints. In one rat study,(8) researchers used a control group and a second group experimentally induced with rheumatoid arthritis. After induction of the condition, an apparent increase in regulation of rCRAMP, the rat analogue of LL-37 peptide, was reported in inflammatory cells. Researchers suggested that LL-37 peptide might induce apoptosis in osteoblasts, potentially leading to decreased bone formation in the joints. The study proposed that increased LL-37 levels may be characteristic of joint inflammation and arthritis and may possibly have diagnostic relevance.
In addition, study(1) suggested that LL-37 elevation may also occur in other inflammatory conditions such as arteriosclerosis. Researchers reported that LL-37 activation and the resulting upregulation of interferons were characteristic of arteriosclerosis-induced cells. Based on these findings, the peptide has been proposed as a possible immunomodulatory research target.
In this study,(9) mice treated with an anti-inflammatory compound were later exposed to LL-37 in order to examine the peptide’s potential role in angiogenesis and wound healing. Researchers suggested that the LL-37-treated mice displayed an apparent increase in vascularization and skin cell formation. The study proposed that LL-37 may stimulate endothelial skin cell proliferation and the formation of tubule-like structures, both of which are important in angiogenesis.
The study also indicated that LL-37 may counteract macrophage activation triggered by lipopolysaccharide (LPS), a component known to provoke immune responses. In addition, LL-37 appeared to support endothelial cell behaviors associated with wound healing, including proliferation, migration, and tubule-like structure formation. Experiments conducted in catabolism-induced murine models using both synthetic and recombinant LL-37 suggested that peptide exposure may enhance vascularization and re-epithelialization. Together, these observations support the hypothesis that LL-37 may play an important role in wound regeneration, potentially through actions related to vascular support.(9)
Studies(10) are ongoing to investigate the potential role of LL-37 in cancer cell development. Some findings have suggested that the peptide may inhibit gastric cancer cell proliferation by activating the bone morphogenetic protein signaling system. The aim of this research has been to explore whether LL-37 might have value as an immunotherapeutic agent or as an adjuvant in efforts to eliminate cancer cells from the host system. CpG oligodeoxynucleotides are widely recognized as immunotherapeutic compounds because they appear to promote tumor-suppressing activity. When combined with LL-37, researchers reported that the peptide appeared to increase the sensitivity of lymphocytes to CpG oligodeoxynucleotides.(10)
LL-37 may also have relevance in research involving gastrointestinal conditions. Increased expression of LL-37 has been observed in experimental models of gastrointestinal ulcers. This upregulation may be mediated by activation of Toll-like receptor 3 (TLR-3) through its ligand, polyinosinic-polycytidylic acid (poly(I)). Poly(I) stimulation may enhance LL-37 expression by activating intracellular signaling cascades involving Toll/IL-1R domain-containing adaptor-inducing interferon (TRIF), tumor necrosis factor receptor-associated factor 6 (TRAF6), and transforming growth factor β-activated kinase 1 (TAK1).
Because of its proposed antimicrobial properties, LL-37 may help protect gastrointestinal mucosa from microbial damage.(12) Its protective role in the GI tract may also involve interactions with lipopolysaccharide (LPS), a component of bacterial cell walls. LL-37 may suppress LPS-induced secretion of pro-inflammatory cytokines such as interleukin-6 (IL-6) and IL-8 in colonic subepithelial myofibroblasts (SEMFs), which may contribute to a protective effect by moderating local inflammation.(12)
LL-37 peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering.
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