Transient binding and dissipation in cross-linked actin networks

Phys Rev Lett. 2008 Sep 5;101(10):108101. doi: 10.1103/PhysRevLett.101.108101. Epub 2008 Sep 5.

Abstract

In contrast with entangled actin solutions, transiently cross-linked actin networks can provide highly elastic properties while still allowing for local rearrangements in the microstructure-on biological relevant time scales. Here, we show that thermal unbinding of transient cross-links entails local stress relaxation and energy dissipation in an intermediate elasticity dominated frequency regime. We quantify the viscoelastic response of an isotropically cross-linked actin network by experimentally tuning the off rate of the transiently cross-linking molecules, their density, and the solvent viscosity. We reproduce the measured frequency response by a semiphenomenological model that is predicated on microscopic unbinding events.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism*
  • Animals
  • Cross-Linking Reagents / pharmacology*
  • Elasticity / drug effects
  • Myosin Subfragments / metabolism
  • Protein Binding / drug effects
  • Rabbits
  • Viscosity / drug effects

Substances

  • Actins
  • Cross-Linking Reagents
  • Myosin Subfragments