[Reaction mechanism of cefotaxime with human serum albumin].
The reaction mechanism of cefotaxime with human serum albumin (HSA) and the affinity between cefotaxime and beta-lactamase were investigated by spectrometry and spectrofluorimetry. The interaction dissociation constants of human serum albumin and cefotaxime were determined from a double reciprocal Lineweaver-Burk plot. The binding distance and transfer efficiency between cefotaxime and HSA were also obtained according to the theory of Förster non-radiation energy transfer. The result suggested that the main binding force between cefotaxime and HSA is electrostatic force interaction. The high beta-lactamase stability of cefotaxime may be correlative with its molecular structure. The antibiotic activity and valence are connected with transfer efficiency and dissociation constant. The effect of cefotaxime on the conformation of HSA was also analyzed using synchronous fluorescence spectrometry.
Liu
Luo-sheng
LS
School of Chemistry and Chemical Engineering, Shandong University, Jinan, China.
Wang
Xing-po
XP
Zhao
Quan-qin
QQ
Zhang
Yu-yi
YY
D000900:Anti-Bacterial Agents / Q000737:chemistry*; D002439:Cefotaxime / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry*
D000900:Anti-Bacterial Agents; D012709:Serum Albumin; D002439:Cefotaxime