LL-37 Peptide – Antimicrobial and Immunomodulatory Research Peptide;
LL-37 peptide is a naturally occurring antimicrobial peptide derived from the human cathelicidin protein (hCAP18). It plays a vital role in the body’s innate immune defense system, acting as a first-line barrier against bacteria, viruses, and fungi.
In research environments, LL-37 is recognized for its antimicrobial, anti-inflammatory, and tissue-regenerative properties. It’s commonly studied in fields like microbiology, immunology, wound healing, and inflammation biology.
As a research compound, LL-37 peptide is for laboratory use only and is not approved for medical or therapeutic use.
2. What Is LL-37 Peptide?
LL-37 is the only human cathelicidin peptide identified to date. It is generated when the precursor protein, hCAP18, is cleaved during immune response activation.
In its natural form, LL-37 circulates in various tissues, including skin, respiratory tract, and immune cells, where it contributes to defense against microbial invaders.
In laboratory settings, synthetic LL-37 peptide is used to study:
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Antimicrobial signaling mechanisms
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Tissue regeneration and wound healing
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Immune cell modulation
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Inflammation and cytokine balance
These properties make LL-37 one of the most versatile research peptides in the study of human immunity and infection control.
3. Chemical Profile and Physical Properties
| Property | Specification |
|---|---|
| Peptide Name | LL-37 (Human Cathelicidin) |
| Sequence | LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES |
| Molecular Formula | C₂₀₃H₃₁₈N₅₆O₄₀ |
| Molecular Weight | ≈ 4493.3 g/mol |
| Appearance | White/off-white lyophilized powder |
| Purity (Research Grade) | ≥ 98% (HPLC verified) |
| Solubility | Water, PBS, or mild acetic acid |
| Storage | −20 °C, desiccated, and light-protected |
| Stability | 24 months (lyophilized) |
4. Mechanism of Action
LL-37 exhibits both direct antimicrobial and immune-modulating activity.
a) Antimicrobial Action
LL-37 disrupts bacterial cell membranes, leading to cell lysis. It acts against gram-positive and gram-negative bacteria, fungi, and even some viruses.
b) Immunomodulation
LL-37 influences immune cell behavior by:
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Regulating cytokine release
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Enhancing macrophage and neutrophil activation
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Supporting tissue regeneration and angiogenesis
c) Wound Healing and Repair
In research, LL-37 has shown potential to:
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Stimulate keratinocyte migration
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Enhance collagen synthesis
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Promote vascular repair and epithelial closure
Its dual action—antimicrobial defense and healing support—makes LL-37 a valuable peptide for inflammation and tissue recovery studies.
5. Research Applications
While LL-37 is not approved for clinical use, it is extensively explored across multiple scientific disciplines.
🧫 1. Antimicrobial Research
LL-37 is a cornerstone peptide in host defense studies, used to examine mechanisms of bacterial resistance and innate immunity.
💪 2. Immune System Modulation
LL-37 is studied for its role in immune regulation, influencing cytokines such as IL-6 and TNF-α.
🩹 3. Wound Healing and Regeneration
Its capacity to promote cell migration, collagen production, and angiogenesis makes it key in tissue repair research.
🧠 4. Inflammatory Conditions
LL-37 may help regulate inflammatory signaling in autoimmune and infection models, helping scientists understand chronic inflammation.
🦠 5. Biofilm and Microbial Defense Studies
Because of its biofilm-disrupting effects, LL-37 is a frequent subject in antimicrobial resistance research.
⚠️ Note: LL-37 peptide is for research use only. It is not for human or veterinary use.
6. Advantages in Research
| Feature | Benefit to Researchers |
|---|---|
| Broad-spectrum antimicrobial | Effective against bacteria, fungi, and viruses |
| Immunomodulatory activity | Balances immune response and inflammation |
| Supports tissue healing | Enhances epithelial repair and angiogenesis |
| Stable synthetic form | High reproducibility and purity for lab use |
| Multi-field relevance | Used in microbiology, immunology, and dermatology studies |
7. Handling and Storage
To preserve LL-37 peptide’s stability and performance:
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Storage: Keep lyophilized powder at −20 °C, sealed, and moisture-free.
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Reconstitution: Use sterile water or phosphate-buffered saline (PBS).
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Handling: Avoid repeated freeze–thaw cycles.
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Labeling: Clearly marked “For Research Use Only – Not for Human Use.”
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Shelf Life: 24 months (unopened, lyophilized).
8. Selecting High-Quality LL-37 Peptide
When sourcing LL-37 peptide for laboratory research, ensure:
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≥ 98% purity verified by HPLC or LC-MS.
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Certificate of Analysis (COA) available for each lot.
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Proper labeling and compliance with research-use standards.
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Temperature-controlled packaging during shipping.
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Transparent synthesis details from a reputable supplier.
High-quality synthesis ensures consistent biological performance in experiments.
9. FAQs – LL-37 Peptide Research
Q1. What is LL-37 peptide?
LL-37 is a human cathelicidin-derived antimicrobial peptide that helps defend against pathogens and supports tissue repair in research models.
Q2. What is LL-37 used for in research?
It is studied for its roles in antimicrobial defense, immune modulation, and wound healing.
Q3. Is LL-37 naturally found in humans?
Yes. It’s the only known human cathelicidin peptide, produced by immune and epithelial cells.
Q4. Can LL-37 be used therapeutically?
No. It is strictly for research use and not approved for medical or clinical applications.
Q5. How is LL-37 stored?
Store at −20 °C, dry and dark, to maintain long-term stability.
10. Summary
LL-37 peptide is one of the most dynamic research peptides known for its antimicrobial and immune-modulating potential. As the only human cathelicidin-derived peptide, it plays a vital role in defense, healing, and immune balance.
In research laboratories, LL-37 continues to provide valuable insights into infection control, skin regeneration, and immune response regulation, making it an indispensable molecule for modern biomedical studies.
Disclaimer: LL-37 peptide is for research and laboratory use only. It is not approved for human or veterinary use.



