Bridging group effects on nearest-neighbor recognition within fluid phospholipid membranes

Langmuir

Volumn 16, Issue 1, 2000, Pages 81-86

  Tokutake, Nobuya ^a   Miyake, Yasuhito ^a   Regen, Steven L ^a  

^a LEHIGH UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIMERS; PHASE TRANSITIONS; POLARIZATION;

DIMYRISTOYL GLYCEROPHOSPHOETHANOLAMINE; DIPHENYL HEXATRIENE; DISTEAROYL GLYCEROPHOSPHOETHANOLAMINE; DITHIODIPROPIONYL; NEAREST-NEIGHBOR RECOGNITION (NNR); PHOSPHOLIPID MEMBRANES;

LIPIDS;

EID: 0033897759     PISSN: 07437463     EISSN: None     Source Type: Journal    
DOI: 10.1021/la990393j     Document Type: Article

References (38)

1. For a detailed discussion of the NNR method, see: Davidson, S. K. M.; Regen, S. L., Chem. Rev. 1997, 97, 1269. Experimentally, a NNR experiment is carried out in the following manner: Two phospholipids (A and B) are first converted into exchangeable, disulfide-linked homodimers (AA and BB) and the corresponding heterodimer (AB). Subsequent vesicle formation, using an equimolar mixture of the two homodimers, followed by monomer exchange via thiolate-disulfide interchange leads to an equilibrium mixture. A similar reaction that is carried out with vesicles made from pure heterodimer ensures that, an equilibrium point has been reached. When the resulting dimer composition is statistical (i.e., when the molar ratio of heterodimer to each homodimer is 2.0) and when there is no driving force for transmembrane asymmetry (i.e., an uneven distribution of phospholipids between the inner and outer monolayer of the bilayer), this finding establishes that the monomeric components are randomly distributed throughout the membrane. When homodimers are favored (i.e., when NNR is present), lateral heterogeneity may or may not exist. If the intramolecular and intermolecular forces within the membrane are similar in magnitude, then NNR also indicates the presence of lateral heterogeneity.
2. (a) Krisovitch, S. M.; Regen, S. L. J. Am. Chem. Soc. 1991, 113, 8175.
3. (b) Krisovitch, S. M.; Regen, S. L. J. Am. Chem. Soc. 1992, 114, 9828.
4. (c) Krisovitch, S. M.; Regen, S. L. J. Am. Chem. Soc. 1993, 115, 1198.
5. (d) Krisovitch, S. M.; Liu, Y.; Regen, S. L. J. Am. Chem. Soc. 1993, 115, 10104.
6. (e) Vigmond, S. J.; Dewa, T.; Regen, S. L. J. Am. Chem. Soc. 1995, 117, 7838.
7. (f) Dewa, T.; Vigmond, S. J.; Regen, S. L. J. Am. Chem. Soc. 1996, 118, 3435.
8. (g) Dewa, T.; Regen, S. L. J. Am. Chem. Soc. 1996, 118, 7069.
9. (h) Dewa, T.; Regen, S. L. J. Am. Chem. Soc. 1996, 118, 8985.
10. (i) Uragami, M.; Dewa, T.; Inagaki, M.; Hendel, R. A.; Regen, S. L. J. Am. Chem. Soc. 1997, 119, 3797.
11. (j) Inagaki, M.; Shibakami, M.; Regen, S. L. J. Am. Chem. Soc. 1997, 119, 7161.
12. (k) Shibakami, M.; Inagaki, M.; Regen, S. L. J. Am. Chem. Soc. 1997, 119, 12354.
13. (l) Shibakami, M.; Inagaki, M.; Regen, S. L. J. Am. Chem. Soc. 1998, 120, 3758.
14. Tocanne, J. F.; Cezanne, L.; Lopez, A.; Piknova, B.; Schram, V.; Tournier, J. F.; Welby, M. Chem. Phys. Lipids 1994, 73, 139.
15. Welti, R.; Glaser, M. Chem. Phys. Lipids 1994, 73, 121.
16. (a) Thompson, T. E.; Sankaram, M. B.; Biltonen, R. L. Comments Mol. Cell. Biophys. 1992, 8, 1.
17. (b) Vaz, W. L. C. Comments Mol. Cell. Biophys. 1992, 8, 17.
18. (c) Glaser, M. Comments Mol. Cell. Biophys. 1992, 8, 37.
19. (d) Tocanne, J. F. Comments Mol. Cell. Biophys. 1992, 8, 53.
20. (e) Edidin, M. Comments Mol. Cell. Biophys. 1992, 8, 73.
21. (f) Wolf, D. E. Comments Mol. Cell. Biophys. 1992, 8, 83.
22. (g) Jesaitis, A. J. Comments Mol. Cell. Biophys. 1992, 8, 97.
23. Gennis, H. B. Biomembranes: Molecular Structure and Function; Springer-Verlag: New York, 1989.
24. For a recent series of papers describing domain formation in biological membranes, see: Mol. Membr. Biol. 1995, 12, 1-162.
25. Radhakrishnan, A.; McConnell, H. M. J. Am. Chem. Soc. 1999, 121, 486.
26. During the course of these studies we found that N-O-1,2,3-benzotriazin-4(3H)one derivatives are more reactive toward amines and that they are also easier to handle than corresponding N-hydroxysuccinimide derivatives: Janout, V.; Lanier, M.; Regen, S. L. Tetrahedron Lett. 1999, 40, 1107.
27. In these experiments, final dimer distributions were obtained from vesicles that were originally composed of pure heterodimer; the final heterodimer/homodimer ratio that was observed starting from vesicles that were composed of an equimolar mixture of homodimers was 1.64 ± 0.04. Repeated attempts to bring about convergence failed. We presume that in the latter dispersion, the homodimers are nonrandomly distributed among the vesicles at the beginning of the exchange and/or transmembrane exists. Since all vesicles that are formed from heterodimer must contain an identical composition and since these membranes must possess transmembrane symmetry, we rely upon data from these vesicles for the determination of true equilibrium mixtures.
28. The fact that product mixtures derived from heterodimer-based vesicles converged with product mixtures derived from 1/1 homodimer-based vesicles, together with the fact that transmembrane movement ("flip-flop") is known to be extremely slow (Ganong, B. R.; Bell, R. M. Biochemistry 1984, 23, 4977.), in and of itself, provides compelling evidence against the presence of transmembrane asymmetry.
29. (a) Burns, J. A.; Butler, J. C.; Moran, J.; Whitesides, G. M. J. Org. Chem. 1991, 8, 2648.
30. (b) Han, J. C.; Han, G. Y. Anal. Biochem. 1994, 220, 5.
31. (a) Gregory, J. D. J. Am. Chem. Soc. 1955, 77, 3922.
32. (b) Beutler, E.; Srivastava, S. K.; West, C. Biochem. Biophys. Res. Commun. 1970, 38, 341.
33. Similar reductions that were carried out with membranes made from 3a and 3c resulted in a reduction of ca. 60% of the dimers. In this case, the molar ratio of 3a/3c fluctuated with time for reasons that we do not presently understand. The extent of heterodimer formation (3b) was also found to be less than that observed from membranes derived from 1a plus 1c, and also 2a plus 2c.
34. Evans, D. F. Langmuir 1988, 4, 3.
35. Israelachvili, J. N.; Jarcelja, S.; Horn, R. G. Q. Rev. Biophys. 1980, 13, 121.
36. New, R. R. C. In Liposomes: A Practical Approach; Oxford University Press: New York, 1989; p 207.
37. VH are the emission intensities that are detected through an analyzer that is oriented parallel and perpendicular to the direction of the vertical polarization of the exciting beam, respectively, and G is a factor that is used to correct for the inability of the instrument to transmit differently polarized light equally. The excitation and emission wavelengths that were used for these measurements were 360 and 430 nm, respectively.
38. Vist, M. R.; Davis, J. H. Biochemistry 1990, 29, 451.