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. 2000 Sep;79(3):1206–1212. doi: 10.1016/s0006-3495(00)76375-2

Model energy landscapes and the force-induced dissociation of ligand-receptor bonds.

T Strunz 1, K Oroszlan 1, I Schumakovitch 1, H Güntherodt 1, M Hegner 1
PMCID: PMC1301017  PMID: 10968985

Abstract

We discuss models for the force-induced dissociation of a ligand-receptor bond, occurring in the context of cell adhesion or single molecule unbinding force measurements. We consider a bond with a structured energy landscape which is modeled by a network of force dependent transition rates between intermediate states. The behavior of a model with only one intermediate state and a model describing a molecular zipper is studied. We calculate the bond lifetime as a function of an applied force and unbinding forces under an increasing applied load and determine the relationship between both quantities. The dissociation via an intermediate state can lead to distinct functional relations of the bond lifetime on force. One possibility is the occurrence of three force regimes where the lifetime of the bond is determined by different transitions within the energy landscape. This case can be related to recent experimental observations of the force-induced dissociation of single avidin-biotin bonds.

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Selected References

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  1. Allen S., Chen X., Davies J., Davies M. C., Dawkes A. C., Edwards J. C., Roberts C. J., Sefton J., Tendler S. J., Williams P. M. Detection of antigen-antibody binding events with the atomic force microscope. Biochemistry. 1997 Jun 17;36(24):7457–7463. doi: 10.1021/bi962531z. [DOI] [PubMed] [Google Scholar]
  2. Anshelevich V. V., Vologodskii A. V., Lukashin A. V., Frank-Kamenetskii M. D. Slow relaxational processes in the melting of linear biopolymers: a theory and its application to nucleic acids. Biopolymers. 1984 Jan;23(1):39–58. doi: 10.1002/bip.360230105. [DOI] [PubMed] [Google Scholar]
  3. Balsera M., Stepaniants S., Izrailev S., Oono Y., Schulten K. Reconstructing potential energy functions from simulated force-induced unbinding processes. Biophys J. 1997 Sep;73(3):1281–1287. doi: 10.1016/S0006-3495(97)78161-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bell G. I. Models for the specific adhesion of cells to cells. Science. 1978 May 12;200(4342):618–627. doi: 10.1126/science.347575. [DOI] [PubMed] [Google Scholar]
  5. Carrion-Vazquez M., Oberhauser A. F., Fowler S. B., Marszalek P. E., Broedel S. E., Clarke J., Fernandez J. M. Mechanical and chemical unfolding of a single protein: a comparison. Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3694–3699. doi: 10.1073/pnas.96.7.3694. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Chang K. C., Hammer D. A. The forward rate of binding of surface-tethered reactants: effect of relative motion between two surfaces. Biophys J. 1999 Mar;76(3):1280–1292. doi: 10.1016/S0006-3495(99)77291-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Dammer U., Hegner M., Anselmetti D., Wagner P., Dreier M., Huber W., Güntherodt H. J. Specific antigen/antibody interactions measured by force microscopy. Biophys J. 1996 May;70(5):2437–2441. doi: 10.1016/S0006-3495(96)79814-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Dammer U., Popescu O., Wagner P., Anselmetti D., Güntherodt H. J., Misevic G. N. Binding strength between cell adhesion proteoglycans measured by atomic force microscopy. Science. 1995 Feb 24;267(5201):1173–1175. doi: 10.1126/science.7855599. [DOI] [PubMed] [Google Scholar]
  9. Evans E. Energy landscapes of biomolecular adhesion and receptor anchoring at interfaces explored with dynamic force spectroscopy. Faraday Discuss. 1998;(111):1–16. doi: 10.1039/a809884k. [DOI] [PubMed] [Google Scholar]
  10. Evans E., Ritchie K. Dynamic strength of molecular adhesion bonds. Biophys J. 1997 Apr;72(4):1541–1555. doi: 10.1016/S0006-3495(97)78802-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Evans E., Ritchie K., Merkel R. Sensitive force technique to probe molecular adhesion and structural linkages at biological interfaces. Biophys J. 1995 Jun;68(6):2580–2587. doi: 10.1016/S0006-3495(95)80441-8. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Evans E., Ritchie K. Strength of a weak bond connecting flexible polymer chains. Biophys J. 1999 May;76(5):2439–2447. doi: 10.1016/S0006-3495(99)77399-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. 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]
  14. Fritz J., Katopodis A. G., Kolbinger F., Anselmetti D. Force-mediated kinetics of single P-selectin/ligand complexes observed by atomic force microscopy. Proc Natl Acad Sci U S A. 1998 Oct 13;95(21):12283–12288. doi: 10.1073/pnas.95.21.12283. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Grubmüller H., Heymann B., Tavan P. Ligand binding: molecular mechanics calculation of the streptavidin-biotin rupture force. Science. 1996 Feb 16;271(5251):997–999. doi: 10.1126/science.271.5251.997. [DOI] [PubMed] [Google Scholar]
  16. Hinterdorfer P., Baumgartner W., Gruber H. J., Schilcher K., Schindler H. Detection and localization of individual antibody-antigen recognition events by atomic force microscopy. Proc Natl Acad Sci U S A. 1996 Apr 16;93(8):3477–3481. doi: 10.1073/pnas.93.8.3477. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Izrailev S., Stepaniants S., Balsera M., Oono Y., Schulten K. Molecular dynamics study of unbinding of the avidin-biotin complex. Biophys J. 1997 Apr;72(4):1568–1581. doi: 10.1016/S0006-3495(97)78804-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Lee G. U., Chrisey L. A., Colton R. J. Direct measurement of the forces between complementary strands of DNA. Science. 1994 Nov 4;266(5186):771–773. doi: 10.1126/science.7973628. [DOI] [PubMed] [Google Scholar]
  19. Merkel R., Nassoy P., Leung A., Ritchie K., Evans E. Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature. 1999 Jan 7;397(6714):50–53. doi: 10.1038/16219. [DOI] [PubMed] [Google Scholar]
  20. Moy V. T., Florin E. L., Gaub H. E. Intermolecular forces and energies between ligands and receptors. Science. 1994 Oct 14;266(5183):257–259. doi: 10.1126/science.7939660. [DOI] [PubMed] [Google Scholar]
  21. Pörschke D. Elementary steps of base recognition and helix-coil transitions in nucleic acids. Mol Biol Biochem Biophys. 1977;24:191–218. doi: 10.1007/978-3-642-81117-3_5. [DOI] [PubMed] [Google Scholar]
  22. Rief M., Gautel M., Oesterhelt F., Fernandez J. M., Gaub H. E. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 1997 May 16;276(5315):1109–1112. doi: 10.1126/science.276.5315.1109. [DOI] [PubMed] [Google Scholar]
  23. Strunz T., Oroszlan K., Schäfer R., Güntherodt H. J. Dynamic force spectroscopy of single DNA molecules. Proc Natl Acad Sci U S A. 1999 Sep 28;96(20):11277–11282. doi: 10.1073/pnas.96.20.11277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Zhu C. Kinetics and mechanics of cell adhesion. J Biomech. 2000 Jan;33(1):23–33. doi: 10.1016/s0021-9290(99)00163-3. [DOI] [PubMed] [Google Scholar]

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