@article {https://doi.org/10.1002/elps.202200279,
	title = {β-Cyclodextrin and folic acid host{\textendash}guest interaction binding parameters determined by Taylor dispersion analysis and affinity capillary electrophoresis},
	journal = {ELECTROPHORESIS},
	volume = {44},
	number = {n/a},
	year = {2023},
	month = {03/2023},
	type = {Research},
	chapter = {in press},
	abstract = {<p>Abstract The thermodynamic properties of molecular recognition in host\&ndash;guest inclusion complexes can be studied by Taylor dispersion analysis (TDA). Host\&ndash;guest inclusion complexes have modest size, and it is possible to get convergent results fast, achieving greater certainty for the obtained thermodynamic properties. Cyclodextrins (CDs) and their derivatives can be used as drug carriers that can boost stability, solubility, and bioavailability of physiologically active substances. A simple and effective approach for assessing the binding properties of CD complexes that are critical in the early stages of drug and formulation development is needed to fully understand the process of CD and guest molecules\&rsquo; complex formation. In this work, TDA was successfully used to rapidly determine interaction parameters, including binding constant and stoichiometry, between β-CD and folic acid (FA) along with the diffusivities of the free FA and its complex with β-CD. Additionally, the FA diffusion coefficient obtained by TDA was compared to the results previously obtained by nuclear magnetic resonance. Affinity capillary electrophoresis (ACE) was also used to compare the binding constants obtained by different methods. The results showed that the binding constants obtained by ACE were somewhat lower than those obtained by the two TDA procedures.</p>},
	keywords = {affinity capillary electrophoresis, binding constant, cyclodextrin, folic acid, Taylor dispersion analysis},
	doi = {https://doi.org/10.1002/elps.202200279},
	url = {https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/abs/10.1002/elps.202200279},
	author = {Dai, Yuanli and Sun, Chang and Yang, Yunhe and Wang, Shuanghao and Li, Huihui and Chen, David D. Y.}
}
@article {FU2019,
	title = {Mass spectrometry and affinity capillary electrophoresis for characterization of host-guest interactions},
	journal = {Journal of Chromatography A},
	volume = {1589},
	year = {2019},
	month = {03/2019},
	pages = {182-190},
	abstract = {<p>Affinity capillary electrophoresis (ACE) in a free solution must be used to confirm the molecular interaction observed in electrospray ionization mass spectrometry (ESI-MS) for affinity binding analysis in the drug discovery process. In this article, the affinity of ibuprofen with three cyclodextrin species of different cavity sizes is investigated by both ESI-MS and ACE methods. Because the binding interactions are measured in different environments using ESI-MS (gas phase) and ACE (liquid phase), the experimental results show significant differences. To better illustrate the major factors influencing the binding constants in different environments, two types of simulations (molecular docking and molecular force field evaluation) are employed in the theoretical discussion. The molecular docking results were consistent with the ESI-MS experimental phenomena. Due to lack of the water molecules in the gas phase, a substantial difference in molecular interaction can contribute to a different binding affinity. By using the molecular modeling based on the force field evaluation with considering solvent molecules, β-CD is expected to form the most stable complex with ibuprofen in the liquid phase and the binding affinity of ibuprofen to γ-CD is much less significant than it is in gas phase. This prediction is in good agreement with the ACE results. Therefore, this work demonstrates that, by using ESI-MS in the first-step screening and ACE in the follow-up determination, a more accurate understanding can be achieved.</p>},
	keywords = {affinity capillary electrophoresis, Electrospray ionization mass spectrometry, Host-guest interaction, molecular modeling},
	issn = {0021-9673},
	doi = {https://doi.org/10.1016/j.chroma.2019.01.020},
	url = {http://www.sciencedirect.com/science/article/pii/S0021967319300202},
	author = {Hengqing Fu and Cheng Qian and Wenjun Tong and Huihui Li and David D.Y. Chen}
}
@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 {397,
	title = {Applications of on-line weak affinity interactions in free solution capillary electrophoresis},
	journal = {Electrophoresis},
	volume = {23},
	number = {6},
	year = {2002},
	note = {ISI Document Delivery No.: 536KNTimes Cited: 26Cited Reference Count: 109},
	month = {Mar},
	pages = {815-822},
	type = {Review},
	abstract = {The impressive selectivity offered by capillary electrophoresis can in some cases be further increased when ligands or additives that engage in weak affinity interactions with one or more of the separated analytes are added to the electrophoresis buffer. This on-line affinity capillary electrophoresis approach is feasible when the migration of complexed molecules is different from the migration of free molecules and when separation conditions are nondenaturing. In this review, we focus on applying weak interactions as tools to enhance the separation of closely related molecules, e.g., drug enantiomers and on using capillary electrophoresis to characterize such interactions quantitatively. We describe the equations for binding isotherms, illustrate how selectivity can be manipulated by varying the additive concentrations, and show how the methods may be used to estimate binding constants. On-line affinity capillary electrophoresis methods are especially valuable for enantiomeric separations and for functional characterization of the contents of biological samples that are only available in minute quantities.},
	keywords = {affinity capillary electrophoresis, ALPHA(1)-ACID, AMYLOID-P COMPONENT, biomolecular interactions, capillary electrophoresis, CHIRAL SEPARATION, CHROMATOGRAPHY, CONSTANTS, ELECTROKINETIC, enantiomer separation, ENANTIOSELECTIVE PROTEIN, FRONTAL ANALYSIS, GLYCOPROTEIN, isotherms, MEASURE BINDING, PARTIAL-FILLING TECHNIQUE, PROTEIN-BINDING, review, separation methods, ZONE-ELECTROPHORESIS},
	isbn = {0173-0835},
	url = {<Go to ISI>://000174699400002},
	author = {Heegaard, N. H. H. and Nissen, M. H. and Chen, D. D. Y.}
}
