LL-37
LL-37 is the only known human cathelicidin antimicrobial peptide, constitutively expressed in neutrophils and induced by infection and vitamin D signaling. It is studied for broad-spectrum antimicrobial defense, immune modulation, biofilm disruption, and potential roles in gut mucosal immunity. Placed on FDA Category 2 list (September 29, 2023) as 'Cathelicidin LL-37.'
Written by WhatPeptide Editorial Team · Last updated 2026-03-17
Half-life
Short; susceptible to protease degradation in vivo
Dosage range
Not established clinically; preclinical studies use mcg-range doses
Administration
Subcutaneous injection
Research level
Preliminary
How LL-37 works
LL-37 disrupts bacterial membranes through electrostatic interactions with anionic lipopolysaccharides, forming pores that cause rapid bacterial lysis across a broad spectrum including antibiotic-resistant strains. Beyond direct antimicrobial activity, LL-37 modulates innate immune responses by acting on formyl peptide receptor-like 1 (FPRL1), promoting chemotaxis of neutrophils and monocytes, and stimulating epithelial wound healing. Its role in gut mucosal defense and modulation of inflammatory bowel conditions is an active area of investigation.
Also known as: Cathelicidin, hCAP-18 C-terminal peptide, CAMP peptide
Research relevance
Side effects & safety
Contraindications
Consult a healthcare provider before use if any of these apply to you.
Key studies
-
Gudmundsson GH et al. — FALL39 gene and processing to LL-37 in granulocytes
First characterization of human cathelicidin gene (FALL39/CAMP); exon 4 encodes mature LL-37
PubMed 1996 -
De Yang et al. — LL-37 utilizes FPRL1 (FPR2) as receptor
LL-37 uses FPR2 (formerly FPRL1) to chemoattract monocytes, neutrophils, and T cells
PubMed 2000 -
Zanetti M et al. — Cathelicidins: novel protein family
Original naming of cathelicidin family; conserved cathelin proregion with variable C-terminal antimicrobial domain
PubMed 1995
FAQ
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