title: Spectrin maintains the lateral order in phosphatidylserine monolayers.
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.
authors.affiliation: School of Physics, University of Exeter, Stocker Road, Exeter, United Kingdom.
authors.forename: J M
authors.initials: JM
authors.lastname: Thompson
authors.forename: R E
authors.initials: RE
authors.lastname: Ellis
authors.forename: E M
authors.initials: EM
authors.lastname: Green
authors.forename: C P
authors.initials: CP
authors.lastname: Winlove
authors.forename: P G
authors.initials: PG
authors.lastname: Petrov
mesh_terms: D021962:Membrane Microdomains / Q000737:chemistry; D010718:Phosphatidylserines / Q000737:chemistry*; D013049:Spectrin / Q000737:chemistry*; D053835:Unilamellar Liposomes / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D010718:Phosphatidylserines; D053835:Unilamellar Liposomes; D013049:Spectrin; C038694:dipalmitoylphosphatidylserine