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Biophys. J. BioFAST: First Published August 19, 2005. doi:10.1529/biophysj.104.051078
© 2005 by the Biophysical Society.

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BIOPHYSICAL THEORY AND MODELING

Anomalous diffusion of proteins due to molecular crowding

Daniel S Banks 1 and Cecile Fradin 1*

1 McMaster University

* To whom correspondence should be addressed. E-mail: fradin{at}physics.mcmaster.ca.

Submitted on August 10, 2004
Revised on October 13, 2004
Accepted on 3 August 2005


  Abstract
We have studied the diffusion of tracer proteins in highly concentrated random-coil polymer and globular protein solutions imitating the crowded conditions encountered in cellular environments. Using fluorescence correlation spectroscopy, we measured the anomalous diffusion exponent {alpha} characterizing the dependence of the mean square displacement of the tracer proteins on time, <r2(t)> ~ t{alpha}. We observed that the diffusion of proteins in dextran solutions with concentrations up to 400g/l is subdiffusive ({alpha}< 1) even at low obstacle concentration. The anomalous diffusion exponent {alpha} decreases continuously with increasing obstacle concentration and molecular weight, but does not depend on buffer ionic strength, neither does it depend strongly on solution temperature. At very high random-coil polymer concentrations, {alpha} reaches a limit value of {alpha}l {approx} 3/4, which we take to be the signature of a coupling between the motions of the tracer proteins and the segments of the dextran chains. A similar, although less pronounced, subdiffusive behavior is observed for the diffusion of streptavidin in concentrated globular protein solutions. These observations indicate that protein diffusion in the cell cytoplasm and nucleus should be anomalous as well, with consequences for measurements of solute diffusion coefficients in cells and for the modeling of cellular processes relying on diffusion.

Key Words: Subdiffusion, dextran, fluorescence correlation spectroscopy, intracellular trafficking, macromolecular crowding, polymer solutions




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Copyright © 2005 by the Biophysical Society.