Spectrin maintains the lateral order in phosphatidylserine monolayers |
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Authors: | Thompson J M Ellis R E Green E M Winlove C P Petrov P G |
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Institution: | School of Physics, University of Exeter, Stocker Road, Exeter, United Kingdom. |
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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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Keywords: | Lipid monolayers Spectrin X-ray diffraction Red blood cell Rafts Membrane skeleton |
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