Skip to main content
PMC home page
Biophysical Journal logoLink to Biophysical Journal
. 1994 Mar;66(3 Pt 1):898–911. doi: 10.1016/s0006-3495(94)80866-5

Theory for measuring bivalent surface binding kinetics using total internal reflection with fluorescence photobleaching recovery.

H V Hsieh 1, N L Thompson 1
PMCID: PMC1275788  PMID: 8011922

Abstract

Total internal reflection with fluorescence photobleaching recovery (TIR-FPR) is a method for experimentally examining coupled diffusion and reaction kinetics at surfaces. In a previous work (Thompson et al. 1981. Biophys. J. 33:435-454), a theoretical basis for interpreting TIR-FPR data was described for monovalent ligands that undergo a reversible reaction with monovalent surface sites in a single step. Here, the theory for TIR-FPR has been extended to two different surface binding mechanisms that involve sequential, bivalent surface attachment. Methods for obtaining the intrinsic surface association and dissociation kinetic rates from measured fluorescence photobleaching recovery curves are described. The new theory should be applicable to the association of bivalent protein ligands such as antibodies with supported planar model membranes.

Full text

PDF
898

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Abney J. R., Scalettar B. A., Thompson N. L. Evanescent interference patterns for fluorescence microscopy. Biophys J. 1992 Feb;61(2):542–552. doi: 10.1016/S0006-3495(92)81858-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Axelrod D., Koppel D. E., Schlessinger J., Elson E., Webb W. W. Mobility measurement by analysis of fluorescence photobleaching recovery kinetics. Biophys J. 1976 Sep;16(9):1055–1069. doi: 10.1016/S0006-3495(76)85755-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Berg H. C., Purcell E. M. Physics of chemoreception. Biophys J. 1977 Nov;20(2):193–219. doi: 10.1016/S0006-3495(77)85544-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Burghardt T. P., Axelrod D. Total internal reflection/fluorescence photobleaching recovery study of serum albumin adsorption dynamics. Biophys J. 1981 Mar;33(3):455–467. doi: 10.1016/S0006-3495(81)84906-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Davoust J., Devaux P. F., Leger L. Fringe pattern photobleaching, a new method for the measurement of transport coefficients of biological macromolecules. EMBO J. 1982;1(10):1233–1238. doi: 10.1002/j.1460-2075.1982.tb00018.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Dembo M., Goldstein B. Theory of equilibrium binding of symmetric bivalent haptens to cell surface antibody: application to histamine release from basophils. J Immunol. 1978 Jul;121(1):345–353. [PubMed] [Google Scholar]
  7. Erickson J., Goldstein B., Holowka D., Baird B. The effect of receptor density on the forward rate constant for binding of ligands to cell surface receptors. Biophys J. 1987 Oct;52(4):657–662. doi: 10.1016/S0006-3495(87)83258-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Goldstein B., Posner R. G., Torney D. C., Erickson J., Holowka D., Baird B. Competition between solution and cell surface receptors for ligand. Dissociation of hapten bound to surface antibody in the presence of solution antibody. Biophys J. 1989 Nov;56(5):955–966. doi: 10.1016/S0006-3495(89)82741-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kaufman E. N., Jain R. K. Measurement of mass transport and reaction parameters in bulk solution using photobleaching. Reaction limited binding regime. Biophys J. 1991 Sep;60(3):596–610. doi: 10.1016/S0006-3495(91)82089-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Müller B., Zerwes H. G., Tangemann K., Peter J., Engel J. Two-step binding mechanism of fibrinogen to alpha IIb beta 3 integrin reconstituted into planar lipid bilayers. J Biol Chem. 1993 Mar 25;268(9):6800–6808. [PubMed] [Google Scholar]
  11. Ortega E., Schweitzer-Stenner R., Pecht I. Kinetics of ligand binding to the type 1 Fc epsilon receptor on mast cells. Biochemistry. 1991 Apr 9;30(14):3473–3483. doi: 10.1021/bi00228a018. [DOI] [PubMed] [Google Scholar]
  12. Pearce K. H., Hiskey R. G., Thompson N. L. Surface binding kinetics of prothrombin fragment 1 on planar membranes measured by total internal reflection fluorescence microscopy. Biochemistry. 1992 Jul 7;31(26):5983–5995. doi: 10.1021/bi00141a005. [DOI] [PubMed] [Google Scholar]
  13. Pearce K. H., Hof M., Lentz B. R., Thompson N. L. Comparison of the membrane binding kinetics of bovine prothrombin and its fragment 1. J Biol Chem. 1993 Nov 5;268(31):22984–22991. [PubMed] [Google Scholar]
  14. Pisarchick M. L., Gesty D., Thompson N. L. Binding kinetics of an anti-dinitrophenyl monoclonal Fab on supported phospholipid monolayers measured by total internal reflection with fluorescence photobleaching recovery. Biophys J. 1992 Jul;63(1):215–223. doi: 10.1016/S0006-3495(92)81592-8. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Pisarchick M. L., Thompson N. L. Binding of a monoclonal antibody and its Fab fragment to supported phospholipid monolayers measured by total internal reflection fluorescence microscopy. Biophys J. 1990 Nov;58(5):1235–1249. doi: 10.1016/S0006-3495(90)82464-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Schmidt C. F., Zimmermann R. M., Gaub H. E. Multilayer adsorption of lysozyme on a hydrophobic substrate. Biophys J. 1990 Mar;57(3):577–588. doi: 10.1016/S0006-3495(90)82573-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Tilton R. D., Gast A. P., Robertson C. R. Surface diffusion of interacting proteins. Effect of concentration on the lateral mobility of adsorbed bovine serum albumin. Biophys J. 1990 Nov;58(5):1321–1326. doi: 10.1016/S0006-3495(90)82473-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Weis R. M., Balakrishnan K., Smith B. A., McConnell H. M. Stimulation of fluorescence in a small contact region between rat basophil leukemia cells and planar lipid membrane targets by coherent evanescent radiation. J Biol Chem. 1982 Jun 10;257(11):6440–6445. [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES