title: Biophysical study on the interaction of ceftriaxone sodium with bovine serum albumin using spectroscopic methods.
abstract: The interaction of ceftriaxone sodium (CS), a cephalosporin antibiotic, with the major transport protein, bovine serum albumin (BSA), was investigated using different spectroscopic techniques such as fluorescence, circular dichroism (CD), and UV-vis spectroscopy. Values of binding parameters for BSA-CS interaction in terms of binding constant and number of binding sides were found to be 9.00 × 10(3), 3.24 × 10(3), and 2.30 × 10(3) M(-1) at 281, 301, and 321 K, respectively. Thermodynamic analysis of the binding data obtained at different temperatures showed that the binding process was spontaneous and was primarily mediated by van der Waals force or hydrogen bonding. CS binding to BSA caused secondary structural alterations in the protein as revealed by CD results. The distance between CS and Trp of BSA was determined as 3.23 nm according to the Förster resonance energy transfer theory.
authors.affiliation: Department of Respiration, Lishui People's Hospital, Zhejiang, Lishui 323000, People's Republic of China.
authors.forename: Jiongwei
authors.initials: J
authors.lastname: Pan
authors.forename: Zaiting
authors.initials: Z
authors.lastname: Ye
authors.forename: Xiaoping
authors.initials: X
authors.lastname: Cai
authors.forename: Liangxing
authors.initials: L
authors.lastname: Wang
authors.forename: Zhuo
authors.initials: Z
authors.lastname: Cao
mesh_terms: D001665:Binding Sites; D001703:Biophysics; D002443:Ceftriaxone / Q000737:chemistry*; D002942:Circular Dichroism; D005453:Fluorescence; D006860:Hydrogen Bonding; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013057:Spectrum Analysis / Q000379:methods*; D013816:Thermodynamics
chemical_list: D012710:Serum Albumin, Bovine; D002443:Ceftriaxone