INVESTIGADORES
FRIAS Maria De Los Angeles
artículos
Título:
LYSO PHOSPHATIDYLCHOLINE-ARBUTIN COMPLEXES FORM BILAYER-LIKE STRUCTURES.
Autor/es:
FRIAS, M DE LOS ANGELES; WINIK,B.; FRANZONI, M.B.; LEVSTEIN, P.R.; NICASTRO, AL; GENNARO, A.M.; DIAZ, S.B.; DISALVO, E.A.
Revista:
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Editorial:
Elsevier
Referencias:
Año: 2008 vol. 1778 p. 1259 - 1266
ISSN:
0005-2736
Resumen:
The association of monomyristoylphosphatidylcholine (14:0 lysoPC) with arbutin forms particles of c.a. 6 nm in diameter as shown by Electron Microscopy.  A 1:1 lysoPC/ arbutin molar ratio shows a 31P NMR 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 array. FTIR spectroscopy shows that arbutin interacts with the hydrated population of the carbonyl groups and with the phosphates through the formation of hydrogen bonds. It is interpreted that hydrophobic interactions among the phenol group of arbutin and the acyl chain of lysoPC are responsible for the decrease in acyl chain mobility observed at the 5th C level by EPR. A model proposing the formation of interdigitated bilayers of arbutin-lysoPC could explain the experimental results.