Salt dependence on vancomycin-herbicide enantiomer binding: capillary electrophoresis study and theoretical approach.
In a previous paper, a mathematical model was developed for the estimation of binding constants by capillary electrophoresis (Guillaume and Peyrin, Anal. Chem. 1999, 71, 2046-2052). This model was applied to determinate the binding constant of the guest-vancomycin complex as well as the degree of complexation n(c) (percent of complexed guest). In this work, the guest molecule were a series of acid herbicide enantiomers (aryloxypropionic, aryloxyphenoxypropionic, and aminopropionic acid). The effects of the run buffer salt concentration on the herbicide-vancomycin binding was clearly described by the determination of specific physicochemical parameters as well as thermodynamic data. These results demonstrate that a better understanding of the interactions involved in the guest molecule-vancomycin binding allows to optimize the enantiomeric separation of this chiral guest molecule.
André
Claire
C
Equipe des Sciences Séparatives et Biopharmaceutiques (2SB), Laboratoire de Chimie Analytique, Faculté de Médecine Pharmacie, Besançon, France.
Guillaume
Yves-Claude
YC
D019075:Electrophoresis, Capillary / Q000379:methods*; D006540:Herbicides / Q000737:chemistry*; D015203:Reproducibility of Results; D012492:Salts / Q000737:chemistry*; D013237:Stereoisomerism; D013696:Temperature; D014640:Vancomycin / Q000737:chemistry*
D006540:Herbicides; D012492:Salts; D014640:Vancomycin