LL-37 Research Profile: Investigating Cathelicidin-Mediated Membrane Permeabilization

LL-37 ( $LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES$ ) represents the linear, amphipathic alpha-helical C-terminal fragment of the human cathelicidin antimicrobial peptide (hCAP18). In 2026 life sciences research, this 37-amino acid biomolecule serves as a foundational model for examining innate immune signaling, cytokine-independent inflammation modulation, and the physical disruption of anionic lipid bilayers. Institutions choosing to buy LL-37 online trust Peptide Crafters for analytical transparency and batch-specific lab reports.

Molecular Specifications

Parameter	Specification
Amino Acid Sequence	$LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES$
Molecular Formula	$C_{205}H_{340}N_{60}O_{53}$
Molecular Weight	$4493.3\ g/mol$
CAS Number	154947-66-7
Structure	Synthetic amphipathic linear alpha-helical polypeptide (Acetate Salt)
Purity Grade	99%+ Analytical Standard

Pharmacokinetic Horizons

Multimodal Ligand-Receptor Affinity and Lipopolysaccharide Inactivation: LL-37 is heavily utilized for Analyzing the binding affinity at the formyl peptide receptor-like 1 (FPRL1/FPR2) complex and the purinergic P2X7 receptor, tracking how its highly cationic sequence neutralizes bacterial lipopolysaccharides (LPS) to obstruct downstream endotoxin signaling cascades.
Structural Self-Association and Proteolytic Mitigation: The peptide exhibits a unique propensity to self-associate into oligomers under physiological salt concentrations, a biochemical trait that provides intrinsic Proteolytic Mitigation against rapid breakdown by host serine proteases, ensuring sustained baseline structural integrity during long-term incubation assays.
Pro-Inflammatory and Angiogenic Cellular Transduction Flux: Studies focus on the peptide’s secondary Cellular Transduction cascades, specifically mapping the transactivation of the epidermal growth factor receptor (EGFR) and the subsequent upregulation of mitogen-activated protein kinase (MAPK) pathways responsible for modeling angiogenesis and cell migration.

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