Self-limiting aggregation by controlled ligand-receptor stoichiometry

Langmuir

Volumn 16, Issue 6, 2000, Pages 2825-2831

  Kisak, E T ^a   Kennedy, M T ^a   Trommeshauser, D ^a   Zasadzinski, J A ^a  

^a University of California   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AGENTS; AGGLOMERATION; CROSSLINKING; DIFFUSION; LIPIDS; MATHEMATICAL MODELS; ORGANIC COMPOUNDS; REACTION KINETICS; SOLUTIONS; STOICHIOMETRY; SURFACES;

BIOTIN; BIOTIN LIPID FRACTION; COLLOIDAL AGGREGATION; FRACTAL DIMENSION; LIGAND TO RECEPTOR RATIO; LIGANDS; SELF LIMITING AGGREGATION; SMOLUKOWSKI AGGREGATION KINETICS;

COLLOIDS;

EID: 0033893868     PISSN: 07437463     EISSN: None     Source Type: Journal    
DOI: 10.1021/la990787a     Document Type: Article

References (31)

1. Chiruvolu, S.; Walker, S.; Leckband, D.; Israelachvili, J.; Zasadzinski, J. Science 1994, 264, 1753-1756.
2. Walker, S. A.; Kennedy, M. T.; Zasadzinski, J. A. Nature 1997, 387, 61-64.
3. Alivasatos, A. P.; Johnsson, K. P.; Peng, X.; Wilson, T. E.; Loweth, C. J.; Bruder, M. P. J.; Schultz, P. G. Nature 1996, 382, 609-611.
4. Mirkin, C. A.; Letsinger, R. L.; Mucic, R. C.; Storhoff, J. J. Nature 1996, 382, 607-609.
5. Elghanian, R.; Storhoff, J. J.; Mucic, R. C.; Letsinger, R. L.; Mirkin, C. A. Science 1997, 277, 1078-1081.
6. Langer, R.; Vacanti, J. P. Science 1993, 260, 920-926.
7. Lasic, D. D. Liposomes: From Physics to Applications; Elsevier: Amsterdam, 1993.
8. Sackmann, E. Science 1996, 271, 43-48.
9. Allen, T. M. Curr. Opin. Colloid Interface Sci. 1996, 1, 645-651.
10. Fendler, J. Membrane Mimetic Chemistry; John Wiley and Sons: New York, 1983.
11. Wong, J. Y.; Kuhl, T. L.; Israelachvili, J. N.; Mullah, N.; Zalipsky, S. Science 1997, 275, 820-822.
12. Israelachvili, J. N. Intermolecular and Surface Forces, 2nd ed.; Academic Press: London, 1992.
13. Evans, D. F.; Wennerstrom, H. The Colloidal Domain; VCH Publishers: New York, 1994.
14. Lin, M. Y.; Lindsay, H. M.; Weitz, D. A.; Ball, R. C.; Klein, R.; Meakin, P. Nature 1989, 339, 360-362.
15. Lin, M. Y.; Lindsay, H. M.; Weitz, D. A.; Ball, R. C.; Klein, R.; Meakin, P. Phys. Rev. A 1990, 41, 2005-2020.
16. Whitesides, T. H.; Ross, D. S. J. Colloid Interface Sci. 1995, 169, 48-59.
17. Titration of vesicles incorporating 0.16 mol % of biotin-X DHPE with fluorescent BODIPY-labeled avidin or streptavidin (Molecular Probes, Eugene, OR) showed that the fluorescence intensity increased linearly up to a streptavidin to total biotin-lipid mole ratio between 1:8 and 1:9 at which point the fluorescence saturated. As streptavidin has four binding sites per molecule, this shows that roughly one-half of the total biotin-lipids were exposed on the outside of the vesicle. This is consistent with the expected complete miscibility of the biotin-X DHPE with the vesicle phospholipids, leading to a statistical distribution of the biotin-lipid between the inside and outside of the vesicles.
18. Farbman-Yogev, I.; Bohbot-Raviv, Y.; Ben-Shaul, A. J. Phys. Chem. A 1998, 102, 9568-9592.
19. Chiruvolu, S.; Naranjo, E.; Zasadzinski, J. A. In Microstructure of Complex Fluids by Electron Microscopy; Herb, C. A., Prud'homme, R. K., Eds.; ACS Symposium Series 578; American Chemical Society: Washington, DC, 1994.
20. Emans, N.; Biwersi, J.; Verkman, A. S. Biophys. J. 1995, 69, 716-728.
21. B is Boltzman's constant, T is absolute temperature, and η is the solvent viscosity. For ligand-receptor induced aggregation, a much lower rate constant than the diffusion limited one is expected due to the steric requirements of the ligand-receptor bond; the effective rate constant is sometimes written as k = Kσ, in which σ is the probability that a collision will result in binding. σ increases with the biotin-lipid fraction in the vesicle membrane. More complex models have been used to explain the details of the size distributions obtained in diffusion and reaction-limited aggregation (See Lin et al., refs 14 and 15). However, for this model, only the early stages of aggregation are important which are dominated by the reaction limited kinetics, and we assume the simple form of the equations.
22. j are set equal (in the same level of approximation as the original Smolukowski equation), the equations are greatly simplified and an analytical solution is possible.
23. 1, δ decreases relative to R and θ → 1 faster (eq 6).
24. β must start out equal to 1, then decrease to a lower value that likely depends on the streptavidin/biotin ratio. However, good agreement with the fluorescence data (Figure 5) is obtained with δ treated as a fitting parameter, suggesting that β approaches a steady state value.
25. Noppl-Simson, D. A.; Needham, D. Biophys. J. 1996, 70, 1391-1401.
26. Chan, W. C. W.; Nie, S. Science 1998, 281, 2016-2018.
27. Leckband, D. Nature 1995, 376, 617-618.
28. Leckband, D. E.; Schmitt, F.-J.; Isrealachvili, J. N.; Knoll, W. Biochemistry 1994, 33, 4611-4624.
29. Leckband, D.; Muller, W.; Schmitt, F.-J.; Ringsdorf, H. Biophys. J. 1995, 69, 1162-1169.
30. Walker, S. A.; Zasadzinski, J. A. Langmuir 1987, 13, 5076-5081.
31. Weinstein, J. N.; Ralston, E.; Leserman, L. D.; Dragsten, P.; Henkart, P.; Blumenthal, R. Liposome Technol. 1983, 3, 183-205.