LL-37 – 5mg (3ml Pen)

LL-37 is the sole cathelicidin-derived antimicrobial peptide found in humans, and its research profile is genuinely dual-natured. It is studied both as a direct antimicrobial agent and as an immunomodulatory signal, and the literature includes work on contexts where its activity appears beneficial and others where it is implicated in inflammatory pathology. That complexity is what makes it scientifically interesting and what keeps its characterisation unsettled.

LL-37 is a 37-residue cationic amphipathic peptide cleaved from the hCAP18 precursor. Research describes direct antimicrobial activity through electrostatic interaction with negatively charged microbial membranes and subsequent membrane disruption. Beyond direct killing, studies document chemotactic recruitment of immune cells via formyl peptide receptor-like 1, neutralisation of bacterial lipopolysaccharide, and effects on angiogenesis and re-epithelialisation in wound models. Research also implicates the peptide in nucleic acid complex formation relevant to autoimmune inflammatory processes.

A large and mechanistically detailed literature spanning microbiology, immunology and dermatology, including significant work on contexts where the peptide's activity is associated with inflammatory pathology.

Antimicrobial research

In vitro activity against bacterial, fungal and viral targets including biofilm models.

Immune signalling

Studies on chemotaxis, cytokine modulation and LPS neutralisation.

Wound healing

Research on re-epithelialisation and angiogenesis in dermal models.

Inflammatory pathology

Work implicating the peptide in psoriasis and rosacea disease models.

Structural biology

Characterisation of amphipathic helix formation and membrane interaction.