LL-37 (5mg) Peptide – Advanced Antimicrobial Research Peptide in the USA

LL-37 (5mg), also known as Cathelicidin, is a cationic antimicrobial research peptide composed of 37 amino acids. It is naturally expressed in neutrophils and epithelial cells and has become a major focus in laboratory research due to its potential antimicrobial, immunomodulatory, inflammatory, and tissue-repair-related properties.

At Core Peptide, we supply high-purity LL-37 (5mg) peptide exclusively for research and laboratory use to support advanced scientific investigations across the United States.

What Is LL-37 Peptide?

LL-37 peptide is derived from the extracellular cleavage of the human cathelicidin precursor protein hCAP18 by protease enzymes. Once cleaved, LL-37 forms a biologically active α-helical structure with strong cationic properties, which allows it to interact with microbial membranes and cellular targets.

Researchers have noted that LL-37 may form agglomerates and lipid bilayers, potentially protecting the peptide from enzymatic degradation while enabling interactions with bacterial, fungal, and viral membranes.
(Source: National Center for Biotechnology Information – PMC
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3836506/)

LL-37 (5mg) and Antimicrobial Research

Antimicrobial peptides like LL-37 are studied for their ability to interact with pathogens in a non-specific manner, making it difficult for microbes to develop resistance. This property has positioned LL-37 peptide as a valuable research tool in antimicrobial resistance studies.

Multiple studies suggest that LL-37 may first interact electrostatically with microbial membrane lipids, followed by lateral diffusion and peptide assembly. This interaction may lead to:

• Membrane pore formation

• Structural destabilization

• Complete membrane disruption

These mechanisms have been observed in research models involving bacteria, fungi, and certain viral strains, reinforcing LL-37’s importance in antimicrobial peptide research.

LL-37 Peptide and Immune & Inflammatory Response Studies

One of the most studied aspects of LL-37 (5mg) is its role in immune modulation and inflammation. Research has explored how LL-37 interacts with self-nucleic acids released during tissue damage, such as RNA and DNA fragments.

A notable tissue culture study demonstrated that LL-37 combined with U1 RNA significantly increased inflammatory and defense-related gene expression. Researchers suggested that LL-37 may facilitate immune signaling by enabling nucleic acids to bind to scavenger receptors (SRs), triggering clathrin-dependent endocytosis and downstream cytokine production.

This interaction appears to involve receptors such as SR-A6 and SR-B1, which are critical for immune pathway activation. Blocking these receptors significantly reduced cytokine expression, highlighting LL-37’s potential role in immune signaling research.
(Source: Journal of Immunology
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3836506/)

LL-37 Peptide in Autoimmunity Research Models

LL-37 has been extensively studied in autoimmune disease models, particularly psoriasis. Research suggests that endogenous LL-37 may form complexes with DNA, activating type I interferon pathways and contributing to inflammatory cascades.

Interestingly, while LL-37 may enhance inflammation in certain contexts, studies also suggest it may protect keratinocytes from inflammasome activation triggered by cytosolic double-stranded DNA. LL-37-DNA complexes appear not to activate the AIM2 inflammasome, reducing IL-1β secretion.

This dual role highlights the complexity of LL-37 peptide in immune regulation and makes it a valuable research peptide for studying inflammatory balance and autoimmunity mechanisms.

LL-37 (5mg) and Arthritis Research

Research involving animal models of rheumatoid arthritis has demonstrated increased expression of rCRAMP, the rodent analog of LL-37, in inflamed joint tissues. Scientists observed that elevated LL-37 levels were associated with inflammatory cell infiltration and altered bone metabolism.

Some studies suggest that LL-37 may influence osteoblast apoptosis, potentially contributing to decreased bone formation in arthritic joints. These findings have positioned LL-37 peptide as a potential biomarker of inflammation in joint disease research models.

LL-37 Peptide and Tissue Repair Research

LL-37 has also been investigated for its role in angiogenesis and tissue repair. In murine models, LL-37 exposure appeared to enhance:

• Endothelial cell proliferation

• Vascularization

• Skin cell regeneration

These effects are critical components of wound healing and tissue regeneration. Researchers suggest LL-37 may counteract inflammatory macrophage activation while promoting endothelial behaviors necessary for angiogenesis.

This makes LL-37 (5mg) a frequently used peptide in laboratory studies related to wound healing, vascular biology, and tissue repair mechanisms.

LL-37 Peptide and Cancer Cell Research

Ongoing research is evaluating LL-37’s potential role in cancer cell biology. Preliminary studies suggest that LL-37 may inhibit gastric cancer cell proliferation by activating bone morphogenetic protein (BMP) signaling pathways.

Additionally, LL-37 has been explored as a potential immunomodulatory adjuvant, particularly in combination with CpG oligodeoxynucleotides. Researchers observed increased immune sensitivity in lymphocytes when LL-37 was present, indicating potential applications in cancer immunology research.

LL-37 Peptide and Gastrointestinal Research

LL-37 expression has been observed to increase in gastrointestinal ulcer research models. This upregulation may be mediated through Toll-like receptor 3 (TLR-3) signaling pathways.

Due to its antimicrobial characteristics, LL-37 may help protect GI mucosa by interacting with lipopolysaccharides (LPS) and suppressing pro-inflammatory cytokines such as IL-6 and IL-8. These findings support ongoing research into LL-37’s role in gastrointestinal inflammation models.

Chemical Specifications of LL-37 (5mg)

• Molecular Formula: C₂₀₅H₃₄₀N₅₀O₅₃

• Molecular Weight: 4493.34 g/mol

• Alternate Names: Cathelicidin, CAP-18

• Form: Lyophilized peptide (research use only)

Why Buy LL-37 (5mg) from Core Peptide?

Core Peptide USA is a trusted supplier of high-purity research peptides for laboratories and institutions nationwide.

Why researchers choose Core Peptide:

• USA-based peptide supplier

• High-purity research peptides

• Transparent product specifications

• Secure shipping within the United States

• Strict research-only compliance

Explore our full peptide catalog at:
https://corepeptide.us

References

1. Kahlenberg JM, Kaplan MJ. Little peptide, big effects: the role of LL-37 in inflammation and autoimmune disease.
   https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3836506/

2. Seil M et al. Spotlight on Human LL-37, an Immunomodulatory Peptide.
   https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4034075/