Journal
ANALYTICA CHIMICA ACTA
Volume 603, Issue 1, Pages 101-110Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.aca.2007.09.021
Keywords
affinity capillary electrophoresis; separation; fluorescence method; binding constant; fluoroquinolones; human serum albumin
Categories
Ask authors/readers for more resources
The interactions between fluoroquinolones and human serum albumin (HSA) were investigated by affinity capillary electrophoresis (ACE) and fluorescence quenching technique. Based on the efficient separation of several fluoroquinolones using a simple phosphate buffer, the binding constants of fluoroquinolones with HSA were determined simultaneously during one set of electrophoresis by ACE method. The thermodynamic parameters were obtained from data at different temperatures, and the negative Delta H and Delta S values showed that both hydrogen bonds and van der Waals interaction played major roles in the binding of fluoroquinolones to HSA. The interactions were also studied by fluorescence quenching technique. The results of fluorescence titration revealed that fluoroquinolones had the strong ability to quenching the intrinsic fluorescence of HSA through the static quenching procedure. The binding site number n, apparent binding constant K-b and the Stern-Volmer quenching constant K-sv were determined. The thermodynamic parameters were also studied by fluorescence method, and the results were consonant with that of ACE. (C) 2007 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available