Journal
CHEMISTRY AND PHYSICS OF LIPIDS
Volume 151, Issue 1, Pages 66-68Publisher
ELSEVIER IRELAND LTD
DOI: 10.1016/j.chemphyslip.2007.09.003
Keywords
lipid monolayers; spectrin; X-ray diffraction; red blood cell; rafts; membrane skeleton
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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. (C) 2007 Elsevier Ireland Ltd. All rights reserved.
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