Affinity Capillary Electrophoresis in Pharmaceutics and by Reinhard H. H. Neubert, Hans-Hermann Ruttinger

By Reinhard H. H. Neubert, Hans-Hermann Ruttinger

This quantity offers breakthroughs and strategies in affinity capillary electrophoresis to degree and make certain the physicochemical and thermodynamic parameters of drug compounds. It discusses ideas to discover and signify interactions to facilitate advancements in managed drug supply and targeting.

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Affinity Capillary Electrophoresis in Pharmaceutics and Biopharmaceutics (Drugs and the Pharmaceutical Sciences)

This quantity offers breakthroughs and strategies in affinity capillary electrophoresis to degree and ascertain the physicochemical and thermodynamic parameters of drug compounds. It discusses innovations to discover and symbolize interactions to facilitate advancements in managed drug supply and concentrating on.

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D. Micellar Electrochromatography With micelles, microemulsions, or liposomes, a second phase is introduced into the separating system. As in chromatography, exchange of the analyte between the mobile and the stationary phases controls the separation process. Contrary to classical chromatography, both phases are mobile, moving with different velocities. As in all electrophoresis techniques, the net mobility of an analyte is the mean mobility of its fraction in the aqueous and the micellar phases: ␮ = xaqu и ␮aqu ϩ xmic и ␮mic (45) Introduction of micellar electrochromatography by Terabe and coworkers (18) extended the separation power of capillary electrophoresis to uncharged molecules.

2003 by Marcel Dekker, Inc. Fig. 1 Typical binding curve using Eq. (15). Nonlinear regression analysis of a plot of ␮ or Y against [L] provides the association constant KA , and the electrophoretic mobility of the pure complex ␮SL from the experimental data. ␮S corresponds to the substrate mobility at [L] = 0. [L] can be approximated as the added ligand concentration only when the ligand concentration is much greater than the solute concentration or when the binding constant is small. Since all electrophoretic mobility values are proportional to the reciprocal viscosity of the buffer, as derived in Chapter 1, the experimental mobility values ␮ must be normalized to the same buffer viscosity to eliminate all other influences on the experimental data besides the association equilibrium.

During this experiment the high voltage is switched off. In this case the traveling time td of the marker relates to the hydrodynamic flow velocity v at the applied pressure: v= ld td © 2003 by Marcel Dekker, Inc. (16) where ld is the length of the capillary from the injection point to the detector. Viscosity is then calculated using the Hagen–Poiseuilles law (5): ␩= ␲ и⌬pиr 4 8иvиl (17) where l is the total length of the capillary. Since only viscosity ratios have to be determined, only the traveling-time ratios have to be considered, provided that all measurements are done with the same capillary at constant pressure.

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Affinity Capillary Electrophoresis in Pharmaceutics and by Reinhard H. H. Neubert, Hans-Hermann Ruttinger
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