LL-37
Description
LL-37 is a 37 amino acid antimicrobial peptide and the only member of the cathelicidin family found in humans. It is derived from the C-terminal domain of the 18 kDa human cationic antimicrobial protein (hCAP18). Research applications include antimicrobial activity studies and innate immunity research.
Research Summary
LL-37 has been studied for its broad-spectrum antimicrobial activity against bacteria, fungi, and enveloped viruses. Research demonstrates roles beyond direct antimicrobial action, including wound healing promotion, immune cell chemotaxis, and modulation of inflammatory responses. It is the subject of multiple ongoing clinical trials for infectious diseases and wound care.
Mechanism of Action
Disrupts microbial membranes through electrostatic interactions with anionic phospholipids, forming pores that lead to cell lysis. Also activates formyl peptide receptor-like 1 (FPRL1) on immune cells, promoting chemotaxis and cytokine release. Binds LPS to neutralize endotoxin activity.
Known Research Compound Interactions
Based on published preclinical research literature
For laboratory research reference only. Not for human consumption. Interaction data derived from preclinical studies and receptor binding profiles. Always consult primary literature for specific research protocols.
Interaction assessments based on receptor binding affinity, signaling pathway analysis, and published preclinical data. For laboratory research use only. Not for human consumption.
Related Research
Price Comparison
For laboratory research use only. Not for human consumption.
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