@article {1389,
	title = {Behavior of interacting species in capillary electrophoresis described by mass transfer equation},
	journal = {Analytical Chemistry},
	volume = {78},
	number = {6},
	year = {2006},
	note = {ISI Document Delivery No.: 025ZYTimes Cited: 9Cited Reference Count: 30},
	month = {Mar},
	pages = {1832-1840},
	type = {Article},
	abstract = {Affinity capillary electrophoresis (ACE) has been used to estimate thermodynamic constants of binding interactions with linear or nonlinear regression methods. The accuracy of this approach relies heavily on the binding interaction mechanism, which is controlled by both the nature of the interaction and the experimental conditions. The development of a highly efficient computer-simulated ACE system makes it possible to demonstrate the detailed behavior of any interacting species of a given interaction under any conditions. The order of the mobilities of the complex and the two binding species in their free forms is a key factor to determine what molecules in what locations of the column are involved in the interaction, and the peak shape resulting from such interactions, of a given ACE experiment. In this paper and the supporting materials, 18 scenarios in 6 different combinations of migration orders of the free analyte, free additive, and complex formed are studied by a computer simulation program based on the mass transfer equation. From the study of these situations, we conclude high additive concentration (ensuring high capacity factor) and low analyte concentration (ensuring fast fill-in of the free additive in the analyte plug) are crucial for obtaining accurate results when using the regression methods. On the other hand, the approach to estimate binding constants with computer simulation can be much more accurate as long as accurate and efficient simulation models can be developed, especially when the ratio of the additive and analyte concentrations is not large enough.},
	keywords = {BINDING CONSTANTS, CHROMATOGRAPHY, DISPERSION, EFFICIENCY, ERROR PROPAGATION, MONTE-CARLO-SIMULATION, pressure, RECTANGULAR HYPERBOLAE, SEPARATIONS, ZONE-ELECTROPHORESIS},
	isbn = {0003-2700},
	url = {<Go to ISI>://000236307700015},
	author = {Fang, N. and Chen, D. D. Y.}
}
@article {1107,
	title = {Enumeration algorithm for determination of binding constants in capillary electrophoresis},
	journal = {Analytical Chemistry},
	volume = {77},
	number = {8},
	year = {2005},
	note = {ISI Document Delivery No.: 919FZTimes Cited: 11Cited Reference Count: 16},
	month = {Apr},
	pages = {2415-2420},
	type = {Article},
	abstract = {With more accurate simulation models and more efficient algorithms becoming available, the binding constants of an affinity interaction can be obtained from much simpler experiments using capillary electrophoresis. With the enumeration algorithm, all possible combinations of the binding constant and the complex mobility in certain ranges that could result in the experimental migration time of an injected analyte are extracted from a 3-D surface, which depicts the migration times resulting from different values of the binding constant and the mobility of the complex formed between the interacting pair, to form a 2-D curve. When the experimental conditions are changed, the analyte migration time will also change. A new 2-D curve can be constructed from another 3-D surface on the basis of the pairs of binding constants and complex mobility values that could result in the new migration time. Because the true binding constant and complex mobility values have to be the same for both experimental conditions under the same temperature, there has to be a point where both 2-D curves will converge. The coordinates of the converging point give the values for a binding constant and a complex mobility that will fit all 2-D curves generated under certain experimental conditions. p-Nitrophenol is used as the analyte, beta-cyclodextrin is used as the additive, and a one-cell model is used to simulate affinity CE. The experimental conditions that can improve the accuracy of the binding constants are discussed.},
	keywords = {DYNAMIC COMPLEXATION, ERROR PROPAGATION, MIGRATION BEHAVIOR, MONTE-CARLO-SIMULATION, NUMERICAL-SIMULATION, QUANTITATIVE DESCRIPTION, RANGE, RECTANGULAR HYPERBOLAE, SEPARATION, ZONE-ELECTROPHORESIS},
	isbn = {0003-2700},
	url = {<Go to ISI>://000228605100018},
	author = {Fang, N. and Chen, D. D. Y.}
}
@article {620,
	title = {Molecular interaction in capillary electrophoresis},
	journal = {Current Opinion in Biotechnology},
	volume = {14},
	number = {1},
	year = {2003},
	note = {ISI Document Delivery No.: 645XTTimes Cited: 37Cited Reference Count: 22},
	month = {Feb},
	pages = {126-130},
	type = {Review},
	abstract = {At the present time, affinity capillary electrophoresis is a well-established method for the measurement of binding constants involving 1:1 interactions. Many recent applications of this technique have illustrated its versatility. If affinity capillary electrophoresis is to be widely applied to the study of all types of interactions it is imperative that we consider that higher order interactions may be present. Applying proper equations or developing new models appropriate to the description of such systems is essential to obtaining reliable binding information.},
	keywords = {ANALYTE MIGRATION BEHAVIOR, BINDING, CONSTANTS, ERROR PROPAGATION, HUMAN SERUM-ALBUMIN, MONTE-CARLO, RANGE, RECTANGULAR HYPERBOLAE, SIMULATION},
	isbn = {0958-1669},
	url = {<Go to ISI>://000181006300018},
	author = {Galbusera, C. and Chen, D. D. Y.}
}
@article {384,
	title = {Affinity capillary electrophoresis using a low-concentration additive with the consideration of relative mobilities},
	journal = {Analytical Chemistry},
	volume = {74},
	number = {8},
	year = {2002},
	note = {ISI Document Delivery No.: 541BPTimes Cited: 24Cited Reference Count: 28},
	month = {Apr},
	pages = {1903-1914},
	type = {Article},
	abstract = {Most affinity studies in capillary electrophoresis assume that the analyte concentration is much smaller than the additive concentration so that the migration of the analyte has no effect on the concentration of the additive in the capillary. However, in most medium- to high-affinity interactions, the additive concentration has to be kept rather low to observe the changes in analyte mobility before saturation is reached. In this paper, a mathematical model is developed to describe the migration behavior of the analyte in a system where the complex formed becomes concentrated to levels much greater than the original concentration of the additive due to the differences in the mobilities of the analyte, additive, and complex. The analyte is flurbiprofen, the additive is transthyretin, and the stoichiometry of the reaction between the two is 1:2. This study also provides a new algorithm to determine medium- to high-affinity binding interaction constants by CE.},
	keywords = {BINDING, CONSTANTS, DRUG-PROTEIN, ERROR PROPAGATION, LIGANDS, MONTE-CARLO SIMULATION, RANGE, RECTANGULAR HYPERBOLAE, SURFACE-PLASMON RESONANCE, TRANSTHYRETIN},
	isbn = {0003-2700},
	url = {<Go to ISI>://000174965600022},
	author = {Galbusera, C. and Thachuk, M. and De Lorenzi, E. and Chen, D. D. Y.}
}
@article {5087,
	title = {Host-guest binding of simple cavitands in water},
	journal = {Chemical Communications},
	number = {24},
	year = {2001},
	note = {ISI Document Delivery No.: 507TGTimes Cited: 15Cited Reference Count: 37},
	month = {Dec},
	pages = {2680-2681},
	type = {Article},
	abstract = {Simple water soluble cavitands were prepared and the thermodynamics of their binding with neutral guests in water is reported.},
	keywords = {AQUEOUS-SOLUTION, COMPLEXATION, ERROR PROPAGATION, INDUCED-FIT, MEDIA, molecular recognition, MONTE-CARLO SIMULATION, NMR CHEMICAL-SHIFTS, RECTANGULAR HYPERBOLAE, SOLUBLE RESORCIN<4>ARENE},
	isbn = {1359-7345},
	url = {<Go to ISI>://000173044900077},
	author = {Gui, X. and Sherman, J. C.}
}
