LL-37 5mg Research Peptide

LL-37 5mg is a synthetic research peptide and the only known human cathelicidin-derived antimicrobial peptide, composed of 37 amino acids. It is a cationic, alpha-helical peptide naturally generated through the proteolytic cleavage of the precursor protein hCAP18. LL-37 5mg is supplied as a lyophilized powder with a reported purity greater than 99%, intended exclusively for laboratory research use.

What Is LL-37 5mg?

LL-37, also referred to as Cathelicidin or CAP-18, is an endogenous peptide involved in innate immune defense mechanisms. In physiological contexts, it is primarily expressed by neutrophils and epithelial cells. For research purposes, LL-37 5mg is synthesized to allow controlled investigation into antimicrobial peptide structure, membrane interaction, and immune-related signaling pathways.

LL-37 5mg is an experimental research compound and is not approved for human or animal use.

Research Background

Antimicrobial peptides such as LL-37 have been widely studied due to their distinct mode of action compared to conventional antibiotics. Rather than targeting specific enzymatic pathways, these peptides are investigated for their ability to interact directly with microbial membranes through electrostatic and structural mechanisms.

LL-37 is classified as an alpha-helical peptide, a structural feature associated with membrane-binding properties. Research interest centers on understanding how LL-37 contributes to innate immunity and how its physical characteristics influence interactions with bacterial, fungal, and viral model systems in vitro.

Mechanisms of Research Interest

Membrane Interaction

LL-37 5mg has been studied for its ability to associate with negatively charged microbial membranes through electrostatic attraction, followed by lateral diffusion across lipid bilayers.

Membrane Disruption Models

Experimental studies suggest LL-37 may destabilize microbial membranes through mechanisms such as transient pore formation or membrane thinning, leading to loss of membrane integrity in research models.

Structural Stability

Research indicates LL-37 may form peptide agglomerates or associate with lipid bilayers, which could influence its stability and resistance to enzymatic degradation during experimental observation.

These mechanisms are research observations only and do not imply therapeutic or clinical effectiveness.

Molecular and Chemical Information

• Product Name: LL-37 5mg

• Form: Lyophilized powder

• Purity: Greater than 99%

• Amino Acid Length: 37 residues

• Molecular Formula: C205H340N50O53

• Molecular Weight: 4493.34 g/mol

• Alternate Names: Cathelicidin, CAP-18

Research Applications

LL-37 5mg may be utilized by qualified researchers in laboratory studies involving:

• Antimicrobial peptide structure-function analysis

• Innate immune system research

• Membrane interaction and biophysical studies

• Host defense peptide signaling investigations

All use must be limited to controlled research environments.

Regulatory Status and Use Disclaimer

• For research use only

• Not approved by the Food and Drug Administration

• Not intended for human or veterinary use

• Not intended to diagnose, treat, cure, or prevent any disease

• No established clinical safety or efficacy data