LL-37 from Super Human Peptides UK is a synthetic, 37-amino acid peptide. It represents the only member of the cathelicidin family of antimicrobial peptides (AMPs) found naturally in humans, cleaved from the precursor protein hCAP18. In laboratory research, LL-37 is heavily studied for its broad-spectrum antimicrobial, antiviral, and antifungal properties.
Unlike traditional antibiotics, researchers utilize LL-37 to investigate its physical disruption of bacterial cell membranes and its ability to eradicate stubborn biofilms. Furthermore, it serves as a crucial model in immunology for its capacity to neutralize bacterial endotoxins (LPS) and recruit immune cells to sites of tissue damage. Produced under GMP-compliant conditions and verified for 99% purity or higher, LL-37 is an essential tool for advanced infectious disease and innate immunity research.
WarningFor laboratory research use only. Not for human consumption.
Key Features
- —Human Cathelicidin AMP: The primary antimicrobial peptide sequence found in human innate immunity.
- —Broad-Spectrum Activity: Studied against Gram-positive bacteria, Gram-negative bacteria, and fungi.
- —High Purity: 99% purity or higher (verified by HPLC and MS analysis).
- —Quality Standard: GMP / ISO certified manufacturing.
- —Documentation: Full Certificate of Analysis (COA) included with every batch.
Research Focus
- —Antimicrobial Mechanisms: Studying the physical permeabilization and destruction of bacterial membranes.
- —Biofilm Eradication: Researching the peptide's ability to penetrate and dismantle protective bacterial biofilms (e.g., Pseudomonas aeruginosa).
- —Immunomodulation: Investigating the neutralization of lipopolysaccharides (LPS) and the prevention of septic shock in animal models.
- —Chemotaxis: Studies on the recruitment of neutrophils, monocytes, and T-cells to infection sites.
- —Wound Healing: Preclinical models exploring the promotion of angiogenesis (new blood vessel formation) and re-epithelialization in compromised tissues.
Published Research and Study Findings
LL-37 has been the subject of extensive scientific literature regarding the future of combating antibiotic-resistant "superbugs." Laboratory studies demonstrate that LL-37 adopts an alpha-helical structure that allows it to insert directly into the lipid bilayers of pathogens, creating pores that lead to cell death. Beyond its direct killing capacity, research by Bowdish et al.
highlights its profound immunomodulatory effects. In animal models of sepsis, LL-37 has been shown to bind to bacterial endotoxins, dampening the dangerous over-production of pro-inflammatory cytokines while simultaneously stimulating the tissue-repair process. This dual-action profile makes it a highly versatile subject for researchers looking into next-generation wound care and infection-control therapies.
NoteAll findings are derived from laboratory and non-clinical research settings.
Representative Scientific References
- 1.Vandamme, D. et al., "Cathelicidin LL-37: A multifunctional peptide," Cellular Immunology, 2012.
- 2.Bowdish, D.M. et al., "Immunomodulatory properties of defensins and cathelicidins," Current Topics in Microbiology and Immunology, 2006.
- 3.Overhage, J. et al., "Human host defense peptide LL-37 prevents bacterial biofilm formation," Infection and Immunity, 2008.
- 4.Turner, J. et al., "Antimicrobial peptides and their role in human disease," European Journal of Clinical Microbiology and Infectious Diseases, 1998.
