6533b836fe1ef96bd12a0747

RESEARCH PRODUCT

Evaluation of the enantioselective binding of imazalil to human serum albumin by capillary electrophoresis

Yolanda Martín-bioscaSalvador SagradoSalvador SagradoMaría José Medina-hernándezLucía Asensi-bernardiLaura Escuder-gilabert

subject

PharmacologyChromatographybiologyChemistryElutionClinical BiochemistryEnantioselective synthesisSerum albuminGeneral MedicinePlasma protein bindingHuman serum albuminBiochemistryAnalytical ChemistrySulfationCapillary electrophoresisDrug Discoverybiology.proteinmedicineEnantiomerMolecular Biologymedicine.drug

description

In this work, a methodology for the evaluation of enantioselective binding of imazalil (IMA) enantiomers to human serum albumin (HSA) that does not require the separation of free and bound to HSA fractions is developed. This methodology comprises the incubation of IMA–HSA designed mixtures for 30 min directly in the capillary electrophoresis system and the subsequent direct injection and chiral separation of IMA employing highly sulfated β-cyclodextrin as chiral selector and the complete filling technique. Two mathematical approaches were used to estimate apparent affinity constants (K1), protein binding and enantioselectivity (ES) for both enantiomers of IMA. Moderate enantioselective binding of IMA enantiomers to HSA (ES = 2.0) was shown by the 1:1 stoichiometry and log K1 values of 3.4 ± 0.4 and 3.1 ± 0.3 for the first and second eluted enantiomers, respectively. Copyright © 2015 John Wiley & Sons, Ltd.

https://doi.org/10.1002/bmc.3472