OBJECTIVE: To explore the interaction between cefdinir (CE) and bovine serum albumin (BSA) by fluorescence and ultraviolet-visible absorption spectrometry.
 METHODS: Under the optimal conditions, the interaction between CE and BSA was investigated by fluorescence and ultraviolet-visible absorption spectrometry.
 RESULTS: CE could quench (static quenching) the intrinsic fluorescence of BSA by forming the CE-BSA complex. The main binding forces were considered as hydrogen bonds and Van der Waals forces based on the calculated values of the thermodynamic parameter. The process of binding was spontaneous because Gibbs free energy change was negative. The primary binding site for CE was located at sub-domain II of BSA. The values of Hill's coefficients were less than 1, indicating a negative cooperative effect. Synchronous fluorescence spectra showed that the conjugation reaction between CE and BSA did not affect the conformation of BSA, and the binding site was close to the tyrosine residue.
 CONCLUSION This test provides a theoretical basis for revealing the pharmacokinetic issue and the development for new drugs.
Binding Sites ; Cefdinir ; Cephalosporins ; chemistry ; Serum Albumin, Bovine ; chemistry ; Spectrophotometry, Ultraviolet ; Thermodynamics