LL-37 Peptide CAS 597562-32-8

LL-37 Introduction

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The LL-37 Peptide belongs to the cathelicidin family and is the only type of antibacterial peptide discovered in the human body of this family. It is derived from the hCAP-18 precursor protein and is generated through protease cleavage processing. It is distributed in various human cells such as neutrophils and epithelial cells. The commercially available samples are mostly prepared through chemical synthesis or genetic engineering.
This molecule is a amphiphilic α-helical cationic polypeptide with diverse biological activities. On one hand, it can inhibit various microorganisms, including some resistant bacterial strains and viruses; on the other hand, it can participate in immune regulation, recruit immune cells, regulate the body's inflammatory state, and promote epithelial cell migration, accelerating wound repair. Current research has also observed that LL-37 has potential for development in tumor-related research and cholesterol regulation.
At present, the research directions are mostly centered around microbial inhibition, wound repair, immune inflammatory mechanisms, and basic research on tumors. However, LL-37 aMide still has many difficulties in practical applications. It is prone to degradation in the body environment, has certain risks of cell effects, and the preparation cost is high. The industry generally uses methods such as multi-peptide structure modification and new delivery carriers to improve these shortcomings.

What is the mechanism of action of LL-37?

LL-37 Peptide is a cationic amphiphilic α-helical polypeptide that exerts multiple biological effects through electrostatic adsorption, disruption of membrane structure, and regulation of cellular signals.
The positively charged peptide segment can adsorb microbial cell membranes, and the α-helix inserts into the phospholipid layer, causing membrane perforation, resulting in the loss of intracellular substances and inhibiting drug-resistant bacteria and enveloped viruses. The cholesterol content of human cell membranes is high, and it is not affected at normal concentrations. However, at high concentrations, it can damage host cells.
It binds to the FPR2 receptor to recruit immune cells, regulates the release of inflammatory factors, neutralizes lipopolysaccharide stimulation, and maintains the balance of innate immunity. At the same time, it activates the epidermal growth factor pathway, promotes the migration and proliferation of epithelial cells, and assists in the repair of wound tissues.
It can also bind to extracellular nucleic acids to participate in signal transduction, and has potential in the fields of tumor and lipid metabolism research. The activity of LL-37 is affected by concentration, pH, and protease degradation, and the environment can change the conformation and strength of the peptide's action.

What is the function of LL-37?

The application scenarios of LL-37 Peptide can be broadly classified into three categories: basic research, pre-development, and transformation exploration.
In the research scenario, LL-37 is a commonly used reference sample for host defense peptides. It is extensively utilized in various studies related to resistant microorganisms, biofilms, skin wound repair, mucosal immunity, tumor mechanisms, etc., and is frequently used as a tool material for cell experiments and animal models.
In the application exploration stage, there is a greater emphasis on local use. Many studies focus on chronic wounds, skin barrier repair, improvement of oral mucosa status, etc., and conduct related experiments on peptide modification and delivery systems. Due to its characteristics of antibacterial, anti-inflammatory, and facilitating tissue repair, LL-37 also has certain development value in functional raw materials and personal care fields.
At present, there are no mature finished products available on the market. The mainstream supply is mainly in the form of research-grade reagents, which are mainly used for mechanism exploration and early effect evaluation. To further implement, the challenges such as easy degradation, safety boundaries, and preparation costs still need to be overcome.

MF of LL-37

CAS	597562-32-8
Molecular formula	C205H341N61O52
EINECS	200-001-8
Molecular weight	4492.27854
Water solubility	Water: 90 mg/mL (20.03 mM)

Specification

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FAQ: 

Q1:Is LL-37 effective against viruses and fungi?
Effective. In addition to its broad-spectrum antibacterial properties, LL-37 also exhibits antiviral and antifungal activities. It can directly destroy the envelopes of certain viruses, or indirectly inhibit viral and fungal infections by regulating the host's immune system.
Q2:What is the special connection between LL-37 and nucleic acids?

This is a groundbreaking discovery. In the skin lesions of autoimmune diseases such as psoriasis, a high concentration of LL-37 binds to the human body's own DNA to form a complex. This complex can hijack the immune system and is extensively absorbed by immune cells. After that, it strongly stimulates the TLR9 receptor, leading to excessive production of type I interferons and thereby promoting the self-inflammatory response. Moreover, LL-37 can also bind to the double-stranded RNA analogs of viruses, inhibiting their activation of TLR3 and affecting the efficacy of related immunotherapy.

Q3:What potential roles does LL-37 play in cardiovascular diseases?

Studies have shown that in ischemic heart disease, through physical stimulation such as shock wave therapy, LL-37 can be released due to mechanical pressure. These released LL-37 can activate Toll-like receptors, induce vascular regeneration in the heart muscle area, and inhibit scar formation, thereby helping to repair damaged heart tissue.

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