Interactions of diclazuril enantiomers with serum albumins: Multi-spectroscopic and molecular docking approaches.

In this work, multi-spectroscopic and molecular docking methods have been conducted in the investigation of enantioselective interactions between diclazuril enantiomers and human/bovine serum albumins (HSA/BSA). The binding constants between serum albumins (SAs) and diclazuril enantiomers revealed that SAs exhibited stronger binding affinity for (R)-diclazuril than (S)-enantiomer. In addition, the fluorescence quenching of SAs induced by diclazuril enantiomers was ascribed to static quenching mechanism, in which hydrogen bonds and Van der Waals forces were the main interactions.

Reliable HPLC separation, vibrational circular dichroism spectra, and absolute configurations of isoborneol enantiomers.

Resolution of chiral compounds has played an important role in the pharmaceutical field, involving detailed studies of pharmacokinetics, physiological, toxicological, and metabolic activities of enantiomers. Herein, a reliable method by high-performance liquid chromatography (HPLC) coupled with an optical rotation detector was developed to separate isoborneol enantiomers. A cellulose tris(3, 5-dimethylphenylcarbamate)-coated chiral stationary phase showed the best separation performance for isoborneol enantiomers in the normal phase among four polysaccharide chiral packings.