Binding Constants Determination of Ofloxacin and Ornidazole Enantiomers with Sulfated β-Cyclodextrin as Single Ligand by Capillary Electrophoresis using Three Different Linear Plotting Methods
| Autor: | Khaldun M. Al Azzam |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
chemistry.chemical_classification
Chromatography Cyclodextrin Chemistry Ornidazole 010401 analytical chemistry 02 engineering and technology General Chemistry 021001 nanoscience & nanotechnology Ligand (biochemistry) 01 natural sciences 0104 chemical sciences Capillary electrophoresis medicine Ofloxacin Enantiomer 0210 nano-technology medicine.drug |
| Zdroj: | Asian Journal of Chemistry. 33:1663-1670 |
| ISSN: | 0975-427X 0970-7077 |
| DOI: | 10.14233/ajchem.2021.23286 |
| Popis: | The aim of this research is to use capillary electrophoresis to establish/determine the binding constants for ofloxacin and ornidazole enantiomers with the negatively charged chiral selector sulfated-β-cyclodextrin (S-β-CD). Using electrophoretic mobility values of ofloxacin and ornidazole enantiomers at various concentrations of S-β-CD used in the context of background electrolyte (BGE), binding constants were calculated using three separate linearization plots, namely double-reciprocal, X-reciprocal and Y-reciprocal. The R-ofloxacin enantiomer-S-β-CD complex had the highest inclusion affinity of the ofloxacin and ornidazole enantiomers, which matched with previously reported estimation. Every enantiomer-S-β-CD complex’s binding constants, as well as thermodynamic binding parameters, were calculated at different temperatures. The host-guest binding constants using double reciprocal fit showed greater linearity (R2 > 0.99) at all temperature ranges measured (15-30 ºC) as compared to the other two fit approaches. The thermodynamic complexation parameters were found to be dependent on the temperature of the enantiomers, as seen by the linear van’t Hoff (15-30 ºC) plot. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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