Spectrin maintains the lateral order in phosphatidylserine monolayers.
Chem Phys Lipids
; 151(1): 66-8, 2008 Jan.
Article
em En
| MEDLINE
| ID: mdl-17996859
ABSTRACT
We investigate the effect of the skeletal protein spectrin on the lateral order in dipalmitoyl phosphatidylserine monolayers spread on aqueous surfaces using grazing incidence X-ray diffraction. Without spectrin, the condensed lipid monolayer exhibits two-dimensional hexagonal packing, characterized by monotonic decrease in the d-spacing and increase in the degree of order with increasing surface pressure between 17 and 36 mN/m. Addition of spectrin to the aqueous subphase at high pressures preserves the monolayers structural parameters unchanged from 36 to 25 mN/m. These results demonstrate for the first time that spectrin could participate in sustaining the two-dimensional order in lipid domains through a direct interaction with phosphatidylserine species.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfatidilserinas
/
Espectrina
/
Lipossomas Unilamelares
Idioma:
En
Revista:
Chem Phys Lipids
Ano de publicação:
2008
Tipo de documento:
Article
País de afiliação:
Reino Unido