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Updated: Aug 2, 2025

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Fast Force Loading Disrupts Molecular Binding Stability in Human and Mouse Cell Adhesions.

Yunfeng Chen1,2,3, Jiexi Liao4, Zhou Yuan1

  • 1Woodruff School of Mechanical Engineering, Georgia Institute of Technology, Atlanta, Georgia, 30332, USA.

Molecular & Cellular Biomechanics : MCB
|April 17, 2023
PubMed
Summary

Force impacts cell adhesion by altering receptor-ligand bond off-rates. This study reveals force loading rate influences bond stability, reconciling conflicting results from different dynamic force spectroscopy assays with a new model.

Keywords:
Force-regulated molecular bindingbiophysical modelcell adhesiondynamic force spectroscopymechano-signaling

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Area of Science:

  • Biophysics
  • Cellular Mechanics
  • Molecular Interactions

Background:

  • Force is crucial for cell adhesion and mechanosignaling, affecting receptor-ligand bond dissociation rates (off-rates).
  • The precise mechanism by which force regulates these off-rates remains unclear.
  • Discrepancies exist between different dynamic force spectroscopy (DFS) assays (force-clamp vs. force-ramp) when measuring the force-off-rate relationship.

Purpose of the Study:

  • To investigate the mechanism of force-dependent regulation of receptor-ligand bond dissociation.
  • To reconcile contradictory results obtained from different DFS assay methods.
  • To develop a unified biophysical model for bond dissociation under varying force conditions.

Main Methods:

  • Employed a live-cell dynamic force spectroscopy (DFS) technique using a biomembrane force probe.
  • Measured single-bond dissociation in three key receptor-ligand systems: GPIbα-VWF, TCR-OVA peptide:MHC, and αIIbβ3-fibrinogen.
  • Utilized parallel force-clamp and force-ramp assays to compare results.

Main Results:

  • Force loading rate was identified as a critical factor disrupting molecular bond stability.
  • Faster force loading promotes bonds to transition to a faster-dissociating state.
  • A novel biophysical model incorporating force magnitude and loading rate successfully reconciled DFS assay discrepancies across all tested systems.

Conclusions:

  • A new paradigm for understanding force-regulated receptor-ligand interactions has been established.
  • The findings provide guidelines for the appropriate application of different DFS technologies.
  • This work demonstrates the potential of using diverse DFS assays to address specific biological questions in cell adhesion and mechanosignaling.