Glass transition and rheological redundancy in F-actin solutions.
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.
Semmrich
Christine
C
Lehrstuhl für Biophysik E22, Technische Universität München, James-Franck-Strasse, 85748 Garching, Germany.
Storz
Tobias
T
Glaser
Jens
J
Merkel
Rudolf
R
Bausch
Andreas R
AR
Kroy
Klaus
K
D000199:Actins / Q000737:chemistry*; D000818:Animals; D005898:Glass / Q000737:chemistry*; D044367:Phase Transition; D011817:Rabbits; D012212:Rheology; D012996:Solutions; D013696:Temperature
D000199:Actins; D012996:Solutions