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Initial Adsorption Kinetics in a Rectangular Thin Channel, and Coverage-Dependent Structural Transition Observed by Streaming Potential

Philippe Déjardin, Elena N. Vasina

Abstract. One fundamental parameter contributing to the analysis of protein-solid surface interactions is the adsorption kinetic constant ka. For a rectangular channel we give a global representation of the initial experimental adsorption constant k at distance x from the entrance channel, as a function of wall shear rate y, through the variable 1.86 k(x/y)1/3. It is possible to visualize on a single graph the adsorption kinetic constant, the diffusion coefficient, depletion magnitude at the interface, and its thickness relative to that of the transport-limited Lévêque limit. With radiolabeled molecules (with a y emitter like 125I) and well-defined geometries, calibration does not require a known solute diffusion coefficient and is obtained from the abrupt variation of radioactivity at the buffer-protein solution change and vice-versa. Experimental data obtained for the system a-chymotrypsin/mica show that when surface coverage reaches some critical level, the streaming potential becomes almost independent of further interfacial concentration increase; this suggests an interfacial structural transition induced by interactions between adsorbed molecules. Several models based on protein-protein dipolar interactions are proposed.

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