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A mechanically stabilized receptor–ligand flex-bond important in the vasculature

Author

Listed:
  • Jongseong Kim

    (Immune Disease Institute, Harvard Medical School, 3 Blackfan Circle, Boston, Massachusetts 02115, USA)

  • Cheng-Zhong Zhang

    (Immune Disease Institute, Harvard Medical School, 3 Blackfan Circle, Boston, Massachusetts 02115, USA)

  • Xiaohui Zhang

    (Immune Disease Institute, Harvard Medical School, 3 Blackfan Circle, Boston, Massachusetts 02115, USA
    Present address: Bioengineering Program and Mechanical Engineering and Mechanics Dept, Lehigh University, 19 Memorial Drive West, Bethlehem, Pennsylvania 18015a, USA.)

  • Timothy A. Springer

    (Immune Disease Institute, Harvard Medical School, 3 Blackfan Circle, Boston, Massachusetts 02115, USA)

Abstract

'Flex-bonds' aid blood clots Binding of von Willebrand factor to the glycoprotein Ib α subunit on the surface of platelets mediates crosslinking of platelets and is an important factor in blood coagulation. Using a new method that links a receptor together with its ligand in a single molecule to measure the binding and unbinding processes, Kim et al. have identified a previously unrecognized type of bond behaviour. The receptor–ligand bond exists in two distinct states, one seen at low force and a second, more stable state that begins to engage when tensile force is applied, stabilizing it against the force. The discovery of this 'flex-bond' behaviour, involving switching between two populations of slip-bond (with bond lifetimes that decrease with increasing load) rather than catch-bonds (with lifetimes that increase with applied force) has implications for how platelets bound to von Willebrand factor are able to resist force, and for how increased flow activates platelet plug formation.

Suggested Citation

  • Jongseong Kim & Cheng-Zhong Zhang & Xiaohui Zhang & Timothy A. Springer, 2010. "A mechanically stabilized receptor–ligand flex-bond important in the vasculature," Nature, Nature, vol. 466(7309), pages 992-995, August.
    • Handle: RePEc:nat:nature:v:466:y:2010:i:7309:d:10.1038_nature09295
    DOI: 10.1038/nature09295
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