@article {2271,
	title = {Behavior of interacting species in vacancy affinity capillary electrophoresis described by mass balance equation},
	journal = {Electrophoresis},
	volume = {29},
	number = {16},
	year = {2008},
	note = {ISI Document Delivery No.: 343MCTimes Cited: 0Cited Reference Count: 42Sun, Ying Fang, Ning Chen, David D. Y.},
	month = {Aug},
	pages = {3333-3341},
	type = {Article},
	abstract = {Vacancy ACE (VACE) is one of the ACE methods, and has been used to study binding interactions between different biomolecules. Thermodynamic binding constants can be estimated with nonlinear regression methods. With a highly efficient computer simulation program (SimDCCE), it is possible to demonstrate the detailed behaviors of each species during the interaction process under different conditions. In this work, thirteen scenarios in four different combinations of migration orders of the free protein, free drug, and complex formed are studied. The detailed interaction process between protein and ligand is discussed and illustrated based on the mass balance equation, also called mass transfer equation. By properly setting the parameters in the simulation model, the influence of different factors during the interaction process can be well understood.},
	keywords = {affinity capillary electrophoresis, binding constant, COMPUTER-SIMULATION, CONSTANTS, DRUG-PROTEIN-BINDING, equation, EXPERIMENTAL VALIDATION, FRONTAL ANALYSIS, HUMAN-SERUM-ALBUMIN, HUMMEL-DREYER, mass balance, method, PERFORMANCE LIQUID-CHROMATOGRAPHY, vacancy affinity capillary electrophoresis, WALL ADSORPTION, ZONE-ELECTROPHORESIS},
	isbn = {0173-0835},
	url = {<Go to ISI>://000258856900008},
	author = {Sun, Y. and Fang, N. and Chen, D. D. Y.}
}
@article {2270,
	title = {Capillary electrophoresis frontal analysis for characterization of alpha(v)beta(3) integrin binding interactions},
	journal = {Analytical Chemistry},
	volume = {80},
	number = {9},
	year = {2008},
	note = {ISI Document Delivery No.: 295JXTimes Cited: 8Cited Reference Count: 33Sun, Ying Cressman, Sonya Fang, Ning Cullis, Pieter R. Chen, David D. Y.},
	month = {May},
	pages = {3105-3111},
	type = {Article},
	abstract = {The specific binding characteristics of alpha(v)beta(3) integrins with an arginine-glycine-aspartic-acid (RGD) containing fluorescently labeled cyclic peptide is investigated with capillary electrophoresis-frontal analysis method. The new algorithm used to calculate the binding constants and binding stoichiometry was derived without the assumptions made in the commonly used Scatchard Plot method, thus enabling the determination of specific binding parameters in the presence of nonspecific binding. The a,6,3 integrin, a membrane protein, was studied in solution, without the need of immobilization or any other kind of modification. An RGD containing fluorescently labeled cyclic pentapeptide is used as the ligand with both specific and nonspecific binding characteristics, and an arginine-alanine-aspartic-acid (RAD) containing peptide is used as the control for nonspecific binding. While a typical specific binding isotherm has a shape of a rectangular hyperbola, a nonspecific binding isotherm is linear in the same ligand concentration region. A 1:2 specific binding stoichiometry was revealed with the second binding having a similar affinity compared to the first binding event.},
	keywords = {ANGIOGENESIS, BEHAVIOR, CONSTANTS, CYCLIC RGD PEPTIDES, DRUG-PROTEIN-BINDING, INTEGRIN ALPHA(V)BETA(3), PRINCIPLES, RECOGNITION, TRANSDUCTION},
	isbn = {0003-2700},
	url = {<Go to ISI>://000255471900011},
	author = {Sun, Y. and Cressman, S. and Fang, N. and Cullis, P. R. and Chen, D. D. Y.}
}
