文档介绍：
Study on the Interaction Characteristics of Lomefloxacin
and/or Cefazolin with Bovine Serum Albumin by
Spectroscopic Technique#
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Xuyang Liu1,2, Zhihong Shi1,2, Hanwen Sun1,2**
(1. College of Chemical and Environmental Science,Hebei University;
2. Key Laboratory of Analytical Science and Technology of Hebei Province, Baoding , P. R.
)
Abstract: In this paper, the interaction of lomefloxacin (LMF) and/or cefazolin (CFZ) with bovine
serum albumin (BSA) was studied by fluorescence quenching bination with UV-Vis
spectroscopic method under simulative physiological conditions. The fluorescence quenching constants,
binding distance, and binding constants for BSA–LMX and/or CFZ systems were determined. The
fluorescence quenching of BSA by addition of LMF and/or CFZ is due to static quenching and energy
transfer. The ratio of binding constants (KA) for BSA–LMF to BSA–CFZ equals to . In the
presence of CFZ (LMF), the binding distance of BSA-LMF (BSA–CFZ) decreased from to
nm (from to nm), and the binding constant (KA) of BSA–LMF (BSA–CFZ) increased from
×105 to ×105 L/mol (from ×103 to ×104 L/mol). Two-coexisting CFZ and LMF
may lead to the need for more doses to achieve therapeutic effect. Circular dichroism spectra,
synchronous fluorescence, and three-dimensional fluorescence studies showed that the presence of
LMF or CFZ could change the conformation of BSA during the binding process, and the presence of
coexisting LMF and CFZ could change the conformation of BSA further, here LMF was reigning.
Key words: Fluorescence; Bovine serum albumin; Lomefloxacin; Cefazolin; Interaction characteristics
0 Introduction
Serum albumin is one of the most abundant proteins in circulatory system of a wide variety
anisms and one of the most extensively studied proteins at all. The albumins make a
significant contribution to colloid osmotic blood pressure and aid in the transport, dis