title: Glass transition and rheological redundancy in F-actin solutions.
abstract: The unique mechanical performance of animal cells and tissues is attributed mostly to their internal biopolymer meshworks. Its perplexing universality and robustness against structural modifications by drugs and mutations is an enigma in cell biology and provides formidable challenges to materials science. Recent investigations could pinpoint highly universal patterns in the soft glassy rheology and nonlinear elasticity of cells and reconstituted networks. Here, we report observations of a glass transition in semidilute F-actin solutions, which could hold the key to a unified explanation of these phenomena. Combining suitable rheological protocols with high-precision dynamic light scattering, we can establish a remarkable rheological redundancy and trace it back to a highly universal exponential stretching of the single-polymer relaxation spectrum of a "glassy wormlike chain." By exploiting the ensuing generalized time-temperature superposition principle, the time domain accessible to microrheometry can be extended by several orders of magnitude, thus opening promising new metrological opportunities.
authors: Lehrstuhl für Biophysik E22, Technische Universität München, James-Franck-Strasse, 85748 Garching, Germany.
authors: Christine
authors: C
authors: Semmrich
authors: Tobias
authors: T
authors: Storz
authors: Jens
authors: J
authors: Glaser
authors: Rudolf
authors: R
authors: Merkel
authors: Andreas R
authors: AR
authors: Bausch
authors: Klaus
authors: K
authors: Kroy
mesh_terms: D000199:Actins / Q000737:chemistry*; D000818:Animals; D005898:Glass / Q000737:chemistry*; D044367:Phase Transition; D011817:Rabbits; D012212:Rheology; D012996:Solutions; D013696:Temperature
chemical_list: D000199:Actins; D012996:Solutions