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Stability constants of amino acids, peptides, proteins, and other biomolecules determined by CE and related methods: recapitulation of published data
Uselová-Vceláková K, Zusková I, Gas B
Language English Country Germany
Document type Review
- MeSH
- Amino Acids chemistry MeSH
- Electrophoresis, Capillary MeSH
- Electroosmosis MeSH
- Financing, Organized MeSH
- Osmolar Concentration MeSH
- Peptides chemistry MeSH
- Proteins chemistry MeSH
- Drug Stability MeSH
- Thermodynamics MeSH
- Viscosity MeSH
- Publication type
- Review MeSH
The stability (affinity, association, binding, complexation, formation) constant characterizes binding interaction between the analyte and the complexing agent. Knowledge of the stability constant makes possible the prediction and estimation of the binding behavior of constituents (amino acids, peptides, proteins, drugs, antibiotics, enzymes, enantiomers) to their partners, and the finding of a suitable partner for the given analyte to form a stable complex. The present paper summarizes the stability constant determination methods and the approaches used to evaluate the experimental data. Further, the paper recapitulates the published stability constant values determined, mainly, by capillary electrophoretic methods, taken from the Web of Science database covering the last decade. Details of the experimental conditions employed for the determination of the stability constants are also given. The review attempts to give a critical evaluation of the problems that accompany the determination of stability constant and discusses their solution.
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- $a Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, Prague, Czech Republic. vcelakov@natur.cuni.cz
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- $a The stability (affinity, association, binding, complexation, formation) constant characterizes binding interaction between the analyte and the complexing agent. Knowledge of the stability constant makes possible the prediction and estimation of the binding behavior of constituents (amino acids, peptides, proteins, drugs, antibiotics, enzymes, enantiomers) to their partners, and the finding of a suitable partner for the given analyte to form a stable complex. The present paper summarizes the stability constant determination methods and the approaches used to evaluate the experimental data. Further, the paper recapitulates the published stability constant values determined, mainly, by capillary electrophoretic methods, taken from the Web of Science database covering the last decade. Details of the experimental conditions employed for the determination of the stability constants are also given. The review attempts to give a critical evaluation of the problems that accompany the determination of stability constant and discusses their solution.
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