Skip to main content
PMC home page
Biophysical Journal logoLink to Biophysical Journal
. 1999 Mar;76(3):1632–1638. doi: 10.1016/S0006-3495(99)77322-4

Adhesion energy of receptor-mediated interaction measured by elastic deformation.

V T Moy 1, Y Jiao 1, T Hillmann 1, H Lehmann 1, T Sano 1
PMCID: PMC1300139  PMID: 10049343

Abstract

We investigated the role of receptor binding affinity in surface adhesion. A sensitive technique was developed to measure the surface energy of receptor-mediated adhesion. The experimental system involved a functionalized elastic agarose bead resting on a functionalized glass coverslip. Attractive intersurface forces pulled the two surfaces together, deforming the bead to produce an enlarged contact area. The Johnson-Kendall-Roberts (JKR) model was used to relate the surface energy of the interaction to the elasticity of the bead and the area of contact. The surface energies for different combinations of modified surfaces in solution were obtained from reflection interference contrast microscopy (RICM) measurements of the contact area formed by the bead and the coverslip. Studies with surfaces functionalized with ligand-receptor pairs showed that the relationship between surface energy and the association constant of the ligand binding has two regimes. At low binding affinity, surface energy increased linearly with the association constant, while surface energy increased logarithmically with the association constant in the high affinity regime.

Full Text

The Full Text of this article is available as a PDF (104.1 KB).

Selected References

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

  1. Binnig G, Quate CF, Gerber C. Atomic force microscope. Phys Rev Lett. 1986 Mar 3;56(9):930–933. doi: 10.1103/PhysRevLett.56.930. [DOI] [PubMed] [Google Scholar]
  2. Chilkoti A., Boland T., Ratner B. D., Stayton P. S. The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy. Biophys J. 1995 Nov;69(5):2125–2130. doi: 10.1016/S0006-3495(95)80083-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Dembo M., Torney D. C., Saxman K., Hammer D. The reaction-limited kinetics of membrane-to-surface adhesion and detachment. Proc R Soc Lond B Biol Sci. 1988 Jun 22;234(1274):55–83. doi: 10.1098/rspb.1988.0038. [DOI] [PubMed] [Google Scholar]
  4. Diamond M. S., Springer T. A. The dynamic regulation of integrin adhesiveness. Curr Biol. 1994 Jun 1;4(6):506–517. doi: 10.1016/s0960-9822(00)00111-1. [DOI] [PubMed] [Google Scholar]
  5. Dustin M. L., Springer T. A. T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1. Nature. 1989 Oct 19;341(6243):619–624. doi: 10.1038/341619a0. [DOI] [PubMed] [Google Scholar]
  6. Evans E. A. Detailed mechanics of membrane-membrane adhesion and separation. I. Continuum of molecular cross-bridges. Biophys J. 1985 Jul;48(1):175–183. doi: 10.1016/S0006-3495(85)83770-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Evans E., Berk D., Leung A. Detachment of agglutinin-bonded red blood cells. I. Forces to rupture molecular-point attachments. Biophys J. 1991 Apr;59(4):838–848. doi: 10.1016/S0006-3495(91)82296-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Florin E. L., Moy V. T., Gaub H. E. Adhesion forces between individual ligand-receptor pairs. Science. 1994 Apr 15;264(5157):415–417. doi: 10.1126/science.8153628. [DOI] [PubMed] [Google Scholar]
  9. Gingell D., Todd I. Interference reflection microscopy. A quantitative theory for image interpretation and its application to cell-substratum separation measurement. Biophys J. 1979 Jun;26(3):507–526. doi: 10.1016/S0006-3495(79)85268-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Green N. M. Avidin and streptavidin. Methods Enzymol. 1990;184:51–67. doi: 10.1016/0076-6879(90)84259-j. [DOI] [PubMed] [Google Scholar]
  11. Green N. M. Avidin. Adv Protein Chem. 1975;29:85–133. doi: 10.1016/s0065-3233(08)60411-8. [DOI] [PubMed] [Google Scholar]
  12. Green N. M. Thermodynamics of the binding of biotin and some analogues by avidin. Biochem J. 1966 Dec;101(3):774–780. doi: 10.1042/bj1010774. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kuo S. C., Lauffenburger D. A. Relationship between receptor/ligand binding affinity and adhesion strength. Biophys J. 1993 Nov;65(5):2191–2200. doi: 10.1016/S0006-3495(93)81277-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Lauffenburger D. A., Horwitz A. F. Cell migration: a physically integrated molecular process. Cell. 1996 Feb 9;84(3):359–369. doi: 10.1016/s0092-8674(00)81280-5. [DOI] [PubMed] [Google Scholar]
  15. Lawrence M. B., Springer T. A. Leukocytes roll on a selectin at physiologic flow rates: distinction from and prerequisite for adhesion through integrins. Cell. 1991 May 31;65(5):859–873. doi: 10.1016/0092-8674(91)90393-d. [DOI] [PubMed] [Google Scholar]
  16. Leckband D. E., Schmitt F. J., Israelachvili J. N., Knoll W. Direct force measurements of specific and nonspecific protein interactions. Biochemistry. 1994 Apr 19;33(15):4611–4624. doi: 10.1021/bi00181a023. [DOI] [PubMed] [Google Scholar]
  17. Livnah O., Bayer E. A., Wilchek M., Sussman J. L. Three-dimensional structures of avidin and the avidin-biotin complex. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5076–5080. doi: 10.1073/pnas.90.11.5076. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Lollo B. A., Chan K. W., Hanson E. M., Moy V. T., Brian A. A. Direct evidence for two affinity states for lymphocyte function-associated antigen 1 on activated T cells. J Biol Chem. 1993 Oct 15;268(29):21693–21700. [PubMed] [Google Scholar]
  19. Nicholson M. W., Barclay A. N., Singer M. S., Rosen S. D., van der Merwe P. A. Affinity and kinetic analysis of L-selectin (CD62L) binding to glycosylation-dependent cell-adhesion molecule-1. J Biol Chem. 1998 Jan 9;273(2):763–770. doi: 10.1074/jbc.273.2.763. [DOI] [PubMed] [Google Scholar]
  20. Radmacher M., Fritz M., Kacher C. M., Cleveland J. P., Hansma P. K. Measuring the viscoelastic properties of human platelets with the atomic force microscope. Biophys J. 1996 Jan;70(1):556–567. doi: 10.1016/S0006-3495(96)79602-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Sano T., Cantor C. R. Intersubunit contacts made by tryptophan 120 with biotin are essential for both strong biotin binding and biotin-induced tighter subunit association of streptavidin. Proc Natl Acad Sci U S A. 1995 Apr 11;92(8):3180–3184. doi: 10.1073/pnas.92.8.3180. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Schneck J., Maloy W. L., Coligan J. E., Margulies D. H. Inhibition of an allospecific T cell hybridoma by soluble class I proteins and peptides: estimation of the affinity of a T cell receptor for MHC. Cell. 1989 Jan 13;56(1):47–55. doi: 10.1016/0092-8674(89)90982-3. [DOI] [PubMed] [Google Scholar]
  23. Springer T. A. Adhesion receptors of the immune system. Nature. 1990 Aug 2;346(6283):425–434. doi: 10.1038/346425a0. [DOI] [PubMed] [Google Scholar]
  24. Springer T. A. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell. 1994 Jan 28;76(2):301–314. doi: 10.1016/0092-8674(94)90337-9. [DOI] [PubMed] [Google Scholar]
  25. Sung K. L., Kuhlman P., Maldonado F., Lollo B. A., Chien S., Brian A. A. Force contribution of the LFA-1/ICAM-1 complex to T cell adhesion. J Cell Sci. 1992 Sep;103(Pt 1):259–266. doi: 10.1242/jcs.103.1.259. [DOI] [PubMed] [Google Scholar]
  26. Tözeren A., Mackie L. H., Lawrence M. B., Chan P. Y., Dustin M. L., Springer T. A. Micromanipulation of adhesion of phorbol 12-myristate-13-acetate-stimulated T lymphocytes to planar membranes containing intercellular adhesion molecule-1. Biophys J. 1992 Jul;63(1):247–258. doi: 10.1016/S0006-3495(92)81578-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Weber P. C., Ohlendorf D. H., Wendoloski J. J., Salemme F. R. Structural origins of high-affinity biotin binding to streptavidin. Science. 1989 Jan 6;243(4887):85–88. doi: 10.1126/science.2911722. [DOI] [PubMed] [Google Scholar]

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

RESOURCES