Multi-bead-and-spring model to interpret protein detachment studied by AFM force spectroscopy

Biophys J. 2002 Aug;83(2):706-22. doi: 10.1016/s0006-3495(02)75202-8.

Abstract

This article deals with the detachment of molecules (fibrinogen) from a surface studied experimentally with an atomic force microscope. The detachment (or rupture) forces are measured as a function of the retraction velocity and exhibit a clear dependence on this parameter, even though the interaction between the molecules and the surface are nonspecific. To interpret these data, a mechanical multi-bead-and-spring model is developed. It consists of one to several parallel, "molecular" springs connected to an extra spring representing the cantilever that is moved at constant velocity. The free end of each molecular spring terminates with a particle that interacts with the surface through a Lennard-Jones potential. This Brownian dynamics model is used to analyze the experimental findings. In the framework of this model, it appears that the fibrinogen molecule must be ascribed a stiffness much smaller than that of the cantilever. In addition, several bonds between the molecule and the surface must be taken into account for the range of the molecule-surface interaction not to be unrealistically small. In future work, this model will be extended to more complex mechanisms such as the detachment of cells from a surface.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biophysical Phenomena
  • Biophysics
  • Fibrinogen / chemistry*
  • Humans
  • Microscopy, Atomic Force / methods*
  • Models, Theoretical
  • Protein Conformation
  • Proteins / chemistry*
  • Stress, Mechanical
  • Time Factors

Substances

  • Proteins
  • Fibrinogen