By Reinhard H. H. Neubert, Hans-Hermann Ruttinger
The authors supply suggestions to discover and represent interactions among medicinal drugs, drug cars, and organic membranes to facilitate advancements in managed drug supply and concentrating on. The ebook comprises present functions and methods to spot binding constants among medications, organic constructions, proteins, nucleic acids, and plasmids, raise drug bioavailability, improve the permeability, solubility, energy, and serve as of drug formulations, learn protein-protein exchanges and reactions, and calculate pKa values.
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Additional info for Affinity Capillary Electrophoresis in Pharmaceutics and Biopharmaceutics
REFERENCES 1. 2. 3. 4. 5. 6. KA Connors. Binding Constants. The measurement of molecular complex stability. Wiley, New York, 1987. RHH Neubert, MA Schwarz, Y Mrestani, M Pla¨tzer, K Raith. Afﬁnity capillary electrophoresis in pharmaceutics. Pharm Res 16:1663–1673, 1999. RM Guijt-van Duijn, J Frank, GWK van Dedem, E Baltussen. Recent advances in afﬁnity capillary electrophoresis. Electrophoresis 21:3905–3918, 2000. NHH Heegard, RT Kennedy. Identiﬁcation, quantitation and characterization of biomolecules by capillary electrophoretic analysis of binding interactions.
Solute adsorption can be minimized most effectively by capillary wall coating, thereby decreasing the free energy of hydrophobic or ionic interactions. , addition of Fig. 5 Electropherogram of six sulfur anions illustrating peak fronting [thiosulfate (S2O32Ϫ)] and peak tailing [tetrathionate (S4O2Ϫ 6 )]; for better visibility of peak asymmetry, the perpendicular peak axis is drawn as a solid line. 3. © 2003 by Marcel Dekker, Inc. modiﬁers to the buffer solution; see also Sec. 1). Both methods can be used to eliminate or reverse the charge on the capillary wall, alter hydrophobicity, and, hence, limit solute adsorption.
2003 by Marcel Dekker, Inc. Instead of 3-D plots, traces of the binding isotherm surface through a plane parallel to the [L]/[I] plane (contour diagrams) or proﬁle plots (traces through the /[L] or /[I] plane can be used to explain certain special conditions. Bowser et al. (17) calculated proﬁle plots of binding isotherms assuming the following conditions: KSL = 50 MϪ1, KSI = 50 MϪ1, S = 0 cm2 VϪ1sϪ1, S = 0 cm2 VϪ1sϪ1, SL = 3 ϫ 10Ϫ5 cm2 VϪ1sϪ1, SI = 5 ϫ 10Ϫ5 cm2 VϪ1sϪ1. In Fig. 4, mobility is plotted against [L] at constant concentrations of I.