INVESTIGADORES
DUPUY Fernando Gabriel
congresos y reuniones científicas
Título:
Surface behavior of ceramides with N-acyl chain of different length.
Autor/es:
DUPUY, FERNANDO; FANANI, MARÍA LAURA; MAGGIO, BRUNO
Lugar:
Salta
Reunión:
Congreso; XXXIX Annual Meeting of Argentinean Biophysical Society SAB 2010, workshop CeBEM, structural biology in Latin America, 3rd Latin American Protein Society Meeting; 2010
Institución organizadora:
Sociedad Argentina de Biofísica
Resumen:
Ceramides are
sphingolipids contaning an amine-diol backbone, ussualy C18:1 sphingosine, N-acylated
with fatty acids of different chain length and degree of unsaturation. When
mixed with phospholipids or more complex sphingolipids, long chain ceramides
form laterally segregated condensed domains. Short chain ceramides are widely
used in cell biology studies and were found to mix with phospholipids. In this work,
Langmuir monolayer studies of a series of ceramides N-acylated with fatty acids
of different chain length were carried out, by measuring surface pressure,
surface potential and reflectivity of p-polarized light of the lipids spread at
the air-water interface. Liquid-expanded phases and condensed domains formation
could be observed at 21ºC. The independent parameters measured indicate that
both the morphology of the segregated condensed domains and their relative
thickness are strongly dependent of the N-acyl chain.