Lysophosphatidylcholine-arbutin complexes form bilayer-like structures

FRIAS, M. A.; WINIK, B.; FRANZONI, M. B.; LEVSTEIN, P. R.; NICASTRO, A.; GENNARO, A. M.; DIAZ, S. B.; DISALVO, E. A

Elsevier

Lugar: Amsterdam; Año: 2008 vol. 1778 p. 1259 - 1259

font size="2"> Arbutin is known to suppress melanin production in murine B16 melanoma cells and inhibit phospholipase action. This encourages the possibility to stabilize it in lipid aggregates for its administration in medical applications. Thus, it was of interest to demonstrate that monomyristoylphosphatidylcholine (14:0 lysoPC) and arbutin may form association complexes. This was studied by Electron Microscopy (EM), 31P Nuclear Magnetic Resonance (P-31 NMR), Electronic Paramagnetic Resonance (EPR) and Fourier Transform Infrared Spectroscopy (FTIR). EM images show the formation of particles of c.a. 6 nm in diameter. For a 1:1 lysoPC-arbutin molar ratio P-31 NMR shows a spectrum with a shoulder that resembles the axially symmetric spectrum characteristic of vesicles. The addition of La3+ ions to the arbutin-lysoPC complex allows one to distinguish two phosphorous populations. These results suggest that arbutin-lysoPC forms vesicles with bilayers stabilized in an interdigitated