Monitoring the nucleation of crystalline films of cholesterol on water and in the presence of phospholipid

Journal of Physical Chemistry B

Volumn 102, Issue 5, 1998, Pages

  Lafont, Sylvaine ^a   Rapaport, Hanna ^a   Sömjen, Giora J ^b,c   Renault, Anne ^d   Howes, Paul B ^e   Kjaer, Kristian ^e   Als Nielsen, Jens ^f   Leiserowitz, Leslie ^a   Lahav, Meir ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^b TEL AVIV SOURASKY MEDICAL CENTER   (Israel)

^c TEL AVIV UNIVERSITY   (Israel)

^d LIPHY   (France)

^e TECHNICAL UNIVERSITY OF DENMARK   (Denmark)

^f UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 11744258188     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (27)

1. Gilat, T.; Sömjen, G. J. Biochim. Biophys. Acta 1996, 1286, 95.
2. Sömjen, G. J.; Ringel, Y.; Konikoff, F. M.; Rosenberg, R.; Gilat, T. J. Lipid Res. 1997, 38, 1088.
3. Konikoff, F. M.; Laufer, H.; Messer, G.; Gilat, T. J. Hepatol. 1997, 26, 703.
4. Harvey, P. R.; Sömjen, G.; Gilat, T.; Gallinger, S.; Strasberg, S. M. Biochim. Biophys. Acta 1988, 958, 10.
5. Wang, D. Q. H.; Carey, M. C. J. Lipid Res. 1996, 37, 606-630.
6. Peled, Y.; Halpern, Z.; Eitan, B.; Goldman, G.; Konikoff, F.; Gilat, T. Biochim. Biophys. Acta 1989, 1003, 246.
7. Halpern, Z.; Dudley, M. A.; Lynn, M. P.; Nader, J. M.; Breuer, A. C.; Holzbach, R. T. J. Lipid Res. 1986, 27, 295.
8. Sömjen, G. J.; Coleman, R.; Koch M. H. J.; Wachtel, E.; Billington, D.; Towns-Andrews, T.; Gilat, T. FEBS Lett. 1991, 289, 163.
9. Sömjen, G. J.; Lipka, G.; Schulthess, G.; Koch M. H. J.; Wachtel, E.; Gilat, T.; Hauser, H. Biophys. J. 1995, 68, 1.
10. Finegold, L. Cholesterol in membrane models; CRC Press, Inc.: Boca Raton, FL, 1993; Chapter 4.
11. Subramania, S.; McConnell, H. M. J. Phys. Chem. 1987, 91, 1715.
12. Slotte, J. P. Biochim. Biophys. Acta 1995, 1238, 118.
13. Smaby, J. M.; Brockman, H L.; Brown, R. E. Biochemistry 1994, 33, 9135.
14. Worthman, L.-A. D.; Nag, K.; Davis, P. J.; Keough, K. M. W. Biophys. J. 1997, 72, 2569.
15. z. More detailed descriptions of the GIXD method used for monolayer structure determination are given in: Als-Nielsen, J.; Kjaer, K. Proceedings of The Nato Advanced Study Institute, Phase Transitions in Soft Condensed Matter; Riste, Sherrington, D., Eds.; Plenum Press: New York, Geilo, Norway, 1989; p 113. Als-Nielsen, J.; Jacquemain, D.; Kjaer, K.; Leveiller, F.; Lahav, M.; Leiserowitz, L. Phys. Rep. 1994, 246, 251.
16. z. More detailed descriptions of the GIXD method used for monolayer structure determination are given in: Als-Nielsen, J.; Kjaer, K. Proceedings of The Nato Advanced Study Institute, Phase Transitions in Soft Condensed Matter; Riste, Sherrington, D., Eds.; Plenum Press: New York, Geilo, Norway, 1989; p 113. Als-Nielsen, J.; Jacquemain, D.; Kjaer, K.; Leveiller, F.; Lahav, M.; Leiserowitz, L. Phys. Rep. 1994, 246, 251.
17. D = 1.47 ± 0.06, the calculated thickness of the monolayer was in agreement with the axis length of the cholesterol molecule. The same value was used for all the other ellipsometry analysis (see: Corsel, J. W.; Willems, G. M.; Kop, J. M. M.; Cuypers, P. A.; Hermens, W. Th. J. Colloid Interface Sci. 1986, 111, 544). Ellipsometric angle and surface pressure were recorded simultaneously during compression at 5 °C. Experiments were also performed on films relaxing at a fixed area per molecule.
18. D = 1.47 ± 0.06, the calculated thickness of the monolayer was in agreement with the axis length of the cholesterol molecule. The same value was used for all the other ellipsometry analysis (see: Corsel, J. W.; Willems, G. M.; Kop, J. M. M.; Cuypers, P. A.; Hermens, W. Th. J. Colloid Interface Sci. 1986, 111, 544). Ellipsometric angle and surface pressure were recorded simultaneously during compression at 5 °C. Experiments were also performed on films relaxing at a fixed area per molecule.
19. D = 1.47 ± 0.06, the calculated thickness of the monolayer was in agreement with the axis length of the cholesterol molecule. The same value was used for all the other ellipsometry analysis (see: Corsel, J. W.; Willems, G. M.; Kop, J. M. M.; Cuypers, P. A.; Hermens, W. Th. J. Colloid Interface Sci. 1986, 111, 544). Ellipsometric angle and surface pressure were recorded simultaneously during compression at 5 °C. Experiments were also performed on films relaxing at a fixed area per molecule.
20. D = 1.47 ± 0.06, the calculated thickness of the monolayer was in agreement with the axis length of the cholesterol molecule. The same value was used for all the other ellipsometry analysis (see: Corsel, J. W.; Willems, G. M.; Kop, J. M. M.; Cuypers, P. A.; Hermens, W. Th. J. Colloid Interface Sci. 1986, 111, 544). Ellipsometric angle and surface pressure were recorded simultaneously during compression at 5 °C. Experiments were also performed on films relaxing at a fixed area per molecule.
21. The AFM images were taken on a Topometrix TMX 2010 Discoverer system. Most measurements were made using silicon nitride pyramidal tips on cantilevers of spring constant k ranging between 0.5 and 0.06 N/m. Films were transferred to solid supports (freshly cleaved mica) by the Langmuir-Blodgett technique at 5 °C and examined at room temperature.
22. Assuming a pseudo c-centered rectangular cell, structure factor calculations were performed for the crystalline bilayer that yielded Bragg rod widths compatible with the experimental data.
23. Refined models of the monolayer and bilayer structures will be presented in a forthcoming publication.
24. Craven, B. M. Nature 1976, 260, 727.
25. Li, T.; Massey, I. J.; Swenson, D. C.; Duax, W. L.; Djerassi, C. J. Org. Chem. 1983, 48, 48.
26. The transformation to the subcell may be rationalized since within a layer of the 3D crystal the long-chain axis of the molecules are all parallel and their centers of gravity lie at coordinates (x, y, z), (0.5 + x, y, z), (0.12 + x, 0.44 + y, z), (0.62 + x, 0.44+y. z), where 0.12, 0.44, and 0.62 are sufficiently close to 0, 0.5, 0.5, respectively. The constructed subcell a′ ≈ 1/2(a - b), b′ ≈ 1/2(a + b) embraces a "pseudo" c-centered rectangular cell that resembles the rectangular cell of cholesterol on water, which is "pseudo" c-centered, the Bragg peaks with (h + k) odd being weak (cf. curve C, Figure 1a).
27. Brezesinski, G.; Dietrich, A.; Struth, B.; Böhm, C.; Bouwman, W.; Kjaer, K.; Möhwald, H. Chem. Phys. Lipids 1995, 76, 145.