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Energy landscapes of receptor–ligand bonds explored with dynamic force spectroscopy

Author

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  • R. Merkel

    (University of British Columbia
    Physikdepartment der Technischen Universitt Mnchen)

  • P. Nassoy

    (University of British Columbia
    Physico-Chemie de l'Institut Curie)

  • A. Leung

    (University of British Columbia)

  • K. Ritchie

    (University of British Columbia)

  • E. Evans

    (University of British Columbia
    Biomedical Engineering, Boston University)

Abstract

Atomic force microscopy (AFM)1, 2 has been used to measure the strength of bonds between biological receptor molecules and their ligands3,4,5,6. But for weak noncovalent bonds, a dynamic spectrum of bond strengths is predicted as the loading rate is altered, with the measured strength being governed by the prominent barriers traversed in the energy landscape along the force-driven bond-dissociation pathway7. In other words, the pioneering early AFM measurements represent only a single point in a continuous spectrum of bond strengths, because theory predicts that these will depend on the rate at which the load is applied. Here we report the strength spectra for the bonds between streptavidin (oravidin) and biotin8—the prototype of receptor–ligand interactions used in earlier AFM studies3,4,5, and which have been modelled by molecular dynamics9, 10. We have probed bond formation over six orders of magnitude in loading rate, and find that the bond survival time diminished from about 1 min to 0.001 s with increasing loading rate over this range. The bond strength, meanwhile, increased from about 5 pN to 170 pN. Thus, although they are among the strongest noncovalent linkages in biology (affinity of 1013 to 1015 M−1)8, 11, these bonds in fact appear strong or weak depending on how fast they are loaded. We are also able to relate the activation barriers derived from our strength spectra to the shape of the energy landscape derived from simulations of the biotin–avidin complex.

Suggested Citation

  • R. Merkel & P. Nassoy & A. Leung & K. Ritchie & E. Evans, 1999. "Energy landscapes of receptor–ligand bonds explored with dynamic force spectroscopy," Nature, Nature, vol. 397(6714), pages 50-53, January.
  • Handle: RePEc:nat:nature:v:397:y:1999:i:6714:d:10.1038_16219
    DOI: 10.1038/16219
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    Cited by:

    1. Steffen M Sedlak & Magnus S Bauer & Carleen Kluger & Leonard C Schendel & Lukas F Milles & Diana A Pippig & Hermann E Gaub, 2017. "Monodisperse measurement of the biotin-streptavidin interaction strength in a well-defined pulling geometry," PLOS ONE, Public Library of Science, vol. 12(12), pages 1-16, December.
    2. Alexandre M. J. Gomila & Gonzalo Pérez-Mejías & Alba Nin-Hill & Alejandra Guerra-Castellano & Laura Casas-Ferrer & Sthefany Ortiz-Tescari & Antonio Díaz-Quintana & Josep Samitier & Carme Rovira & Migu, 2022. "Phosphorylation disrupts long-distance electron transport in cytochrome c," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    3. Valentina Lo Schiavo & Philippe Robert & Laurent Limozin & Pierre Bongrand, 2012. "Quantitative Modeling Assesses the Contribution of Bond Strengthening, Rebinding and Force Sharing to the Avidity of Biomolecule Interactions," PLOS ONE, Public Library of Science, vol. 7(9), pages 1-11, September.
    4. Jin Qian & Huajian Gao, 2010. "Soft Matrices Suppress Cooperative Behaviors among Receptor-Ligand Bonds in Cell Adhesion," PLOS ONE, Public Library of Science, vol. 5(8), pages 1-9, August.
    5. Ehsan Akbari & Melika Shahhosseini & Ariel Robbins & Michael G. Poirier & Jonathan W. Song & Carlos E. Castro, 2022. "Low cost and massively parallel force spectroscopy with fluid loading on a chip," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

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