LL-37 5mg

LL-37 is the 37-residue C-terminal fragment of human cathelicidin hCAP-18, the product of the CAMP gene, prepared here by solid-phase synthesis. Its sequence is LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES, and the name records the two N-terminal leucine residues and the chain length. In aqueous buffer at physiological ionic strength the chain adopts an amphipathic α-helical conformation with cationic and hydrophobic residues segregated on opposite faces of the helix.

Two classes of in-vitro target are characterised. Lipid engagement is measured against defined anionic systems — lipopolysaccharide, lipoteichoic acid and liposomes of set composition — by surface plasmon resonance, isothermal titration calorimetry and dye-leakage measurement. Receptor engagement is measured at formyl peptide receptor 2 (FPR2) by radioligand displacement in membranes from FPR2- transfected cells. The reported endpoints are binding constants and permeabilisation values recorded in these defined preparations.

Primary literature describes the solid-phase synthesis of the 37-residue sequence, its circular- dichroism and NMR structural characterisation, and the biophysics of its interaction with defined lipid systems. Search results and cited literature do not establish the performance of a commercial lot or a use recommendation.