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Biophys J, June 2001, p. 2568-2589, Vol. 80, No. 6
Department of Chemistry, Purdue University, West Lafayette, Indiana 47907 USA
The thermodynamics and kinetics of protein adsorption are
studied using a molecular theoretical approach. The cases studied include competitive adsorption from mixtures and the effect of conformational changes upon adsorption. The kinetic theory is based on
a generalized diffusion equation in which the driving force for motion
is the gradient of chemical potentials of the proteins. The
time-dependent chemical potentials, as well as the equilibrium behavior
of the system, are obtained using a molecular mean-field theory. The
theory provides, within the same theoretical formulation, the diffusion
and the kinetic (activated) controlled regimes. By separation of ideal
and nonideal contributions to the chemical potential, the equation of
motion shows a purely diffusive part and the motion of the particles in
the potential of mean force resulting from the intermolecular
interactions. The theory enables the calculation of the time-dependent
surface coverage of proteins, the dynamic surface tension, and the
structure of the adsorbed layer in contact with the approaching
proteins. For the case of competitive adsorption from a solution
containing a mixture of large and small proteins, a variety of
different adsorption patterns are observed depending upon the bulk
composition, the strength of the interaction between the particles, and
the surface and size of the proteins. It is found that the
experimentally observed Vroman sequence is predicted in the case that
the bulk solution is at a composition with an excess of the small
protein, and that the interaction between the large protein and the
surface is much larger than that of the smaller protein. The effect of surface conformational changes of the adsorbed proteins in the time-dependent adsorption is studied in detail. The theory predicts regimes of constant density and dynamic surface tension that are long
lived but are only intermediates before the final approach to
equilibrium. The implications of the findings to the interpretation of
experimental observations is discussed.
Biophys J, June 2001, p. 2568-2589, Vol. 80, No. 6
© 2001 by the Biophysical Society 0006-3495/01/06/2568/22 $2.00
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