title: Cross-linker unbinding and self-similarity in bundled cytoskeletal networks.
abstract: The macromechanical properties of purely bundled in vitro actin networks are not only determined by the micromechanical properties of individual bundles but also by molecular unbinding events of the actin-binding protein (ABP) fascin. Under high mechanical load the network elasticity depends on the forced unbinding of individual ABPs in a rate dependent manner. Cross-linker unbinding in combination with the structural self-similarity of the network enables the introduction of a concentration-time superposition principle--broadening the mechanically accessible frequency range over 8 orders of magnitude.
authors.affiliation: Lehrstuhl für Biophysik E22, Technische Universität München, James-Franck-Strasse 1, 85748 Garching, Germany.
authors.forename: O
authors.initials: O
authors.lastname: Lieleg
authors.forename: A R
authors.initials: AR
authors.lastname: Bausch
mesh_terms: D000199:Actins / Q000737:chemistry; D001696:Biomechanical Phenomena; D002352:Carrier Proteins / Q000737:chemistry; D003432:Cross-Linking Reagents; D003599:Cytoskeleton / Q000648:ultrastructure*; D004548:Elasticity; D007700:Kinetics; D008840:Microfilament Proteins / Q000737:chemistry; D011485:Protein Binding; D014783:Viscosity
chemical_list: D000199:Actins; D002352:Carrier Proteins; D003432:Cross-Linking Reagents; D008840:Microfilament Proteins; C020324:fascin