Probe surface chemistry dependence and local polymer network structure in F-actin microrheology.
We investigate the dependence of F-actin microrheology on probe surface chemistry using diffusing wave spectroscopy. Polystyrene probe particles exhibit subdiffusive mean-squared displacements, where Deltar(2)(t) approximately t(0.77)(+/-)(0.03) consistent with previous experiments and theory. However, polystyrene probes preadsorbed with bovine serum albumin (BSA) interact weakly with the surrounding polymer network and exhibit a scaling exponent similar to pure diffusion Deltar(2)(t) approximately t, which decreases as particle size and actin concentration increases. Using models of particle diffusion in locally heterogeneous viscoelastic microenvironments, we find that the microrheological response of BSA-treated particles is consistent with the formation of a polymer-depleted shell surrounding the probes. The shell thickness scales with particle size but not polymer concentration. These results suggest that the depletion is caused by exclusion or orientation of actin filaments near probes due to their long length and rigidity.
Chae
Byeong Seok
BS
Department of Chemical Engineering, Colburn Laboratory, University of Delaware, Newark, Delaware 19716, USA.
Furst
Eric M
EM
D000199:Actins / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D004548:Elasticity; D011817:Rabbits; D012710:Serum Albumin, Bovine / Q000737:chemistry; D013696:Temperature; D014783:Viscosity
D000199:Actins; D012710:Serum Albumin, Bovine