| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Department of Biochemistry and Pharmacy, Åbo Akademi University, FIN 20521 Turku, Finland
Correspondence: Address reprint requests to J. Peter Slotte, Dept. of Biochemistry and Pharmacy, Åbo Akademi University, PO Box 66, FIN 20521 Turku Finland. Tel.: +358-2-2154689; Fax: +358-2-2154010; E-mail: jpslotte{at}abo.fi0.
The properties of vesicle membranes prepared from 16:0-SM, 16:0-DHSM, or DPPC were characterized using steady-state and time-resolved fluorescence spectroscopy and different fluorescent reporter molecules. The acyl-chain region was probed using free and phospholipid-bound 1,6-diphenyl-1,3,5-hexatriene. 16:0-DHSM was found to be the more ordered than both DPPC and 16:0-SM 5°C below and above melting temperature. Interfacial properties of the phospholipid bilayers were examined using 6-dodecanoyl-2-dimethyl-aminonaphthalene (Laurdan), 6-propionyl-2-dimethyl-amino-naphthalene (Prodan), and dansyl-PE. Laurdan and Prodan reported that the two sphingomyelin (SM) membrane interfaces were clearly different from the DPPC membrane interface, whereas the two SM membrane interfaces had more similar properties (both in gel and liquid-crystalline phase). Prodan partition studies showed that membrane resistance to Prodan partitioning increased in the order: 16:0-SM < DPPC < 16:0-DHSM. The degree to which dansyl-PE is exposed to water reflects the structural properties of the membrane-water interface. By comparing the lifetime of dansyl-PE in water and deuterium oxide solution, we could show that the degree to which the dansyl moiety was exposed to water in the membranes increased in the order: 16:0-SM < DPPC < 16:0-DHSM. In conclusion, this study has shown that DHSM forms more ordered bilayers than acyl-chain matched SM or phosphatidylcholine, even in the liquid-crystalline state.
This article has been cited by other articles:
 |
|
 |
|
  S. P. Soni, D. S. LoCascio, Y. Liu, J. A. Williams, R. Bittman, W. Stillwell, and S. R. Wassall Docosahexaenoic Acid Enhances Segregation of Lipids between Raft and Nonraft Domains: 2H-NMR Study Biophys. J., July 1, 2008; 95(1): 203 - 214. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. Le Guyader, C. Le Roux, S. Mazeres, H. Gaspard-Iloughmane, H. Gornitzka, C. Millot, C. Mingotaud, and A. Lopez Changes of the Membrane Lipid Organization Characterized by Means of a New Cholesterol-Pyrene Probe Biophys. J., December 15, 2007; 93(12): 4462 - 4473. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Margineanu, J.-i. Hotta, M. Van der Auweraer, M. Ameloot, A. Stefan, D. Beljonne, Y. Engelborghs, A. Herrmann, K. Mullen, F. C. De Schryver, et al. Visualization of Membrane Rafts Using a Perylene Monoimide Derivative and Fluorescence Lifetime Imaging Biophys. J., October 15, 2007; 93(8): 2877 - 2891. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. H. Pande, S. Qin, and S. A. Tatulian Membrane Fluidity Is a Key Modulator of Membrane Binding, Insertion, and Activity of 5-Lipoxygenase Biophys. J., June 1, 2005; 88(6): 4084 - 4094. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
F.-X. Contreras, G. Basanez, A. Alonso, A. Herrmann, and F. M. Goni Asymmetric Addition of Ceramides but not Dihydroceramides Promotes Transbilayer (Flip-Flop) Lipid Motion in Membranes Biophys. J., January 1, 2005; 88(1): 348 - 359. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. W. Chiu, S. Vasudevan, E. Jakobsson, R. J. Mashl, and H. L. Scott Structure of Sphingomyelin Bilayers: A Simulation Study Biophys. J., December 1, 2003; 85(6): 3624 - 3636. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. K. M. Nyholm, M. Nylund, and J. P. Slotte A Calorimetric Study of Binary Mixtures of Dihydrosphingomyelin and Sterols, Sphingomyelin, or Phosphatidylcholine Biophys. J., May 1, 2003; 84(5): 3138 - 3146. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
