The Reaction Mechanism between Cefaclox and Human Serum Albumin
Luo-sheng Liu
Abstract
Luo-sheng Liu
Abstract
To study the reaction mechanism between cefaclox and human serum albumin(HSA) in aqueous solution, fluorescence spectra were used. The interaction dissociation constants of human serum albumin and cefaclox were determined from a double reciprocal Lineweaver-Burk plot. The effect of cefaclox on the conformation of HSA was analyzed using synchronous fluorescence spectrometry. The binding distance and transfer efficiency between cefaclox and HSA were also obtained according to the theory of Forster′ non-radiation energy transfer. The main binding force between cefaclox and HSA is hydrophobic interaction. The antibiotic valence is related to the transfer efficiency and dissociation constant.
A significance statement is not available in the OpenAlex record.
A contribution statement is not available in the OpenAlex record.
Method details are not available in the OpenAlex metadata.
Findings are not separately available in the OpenAlex metadata.
Limitations are not available in the OpenAlex metadata.
Application details are not available in the OpenAlex metadata.
To study the reaction mechanism between cefaclox and human serum albumin(HSA) in aqueous solution, fluorescence spectra were used. The interaction dissociation constants of human serum albumin and cefaclox were determined from a double reciprocal Lineweaver-Burk plot. The effect of cefaclox on the conformation of HSA was analyzed using synchronous fluorescence spectrometry. The binding distance and transfer efficiency between cefaclox and HSA were also obtained according to the theory of Forster′ non-radiation energy transfer. The main binding force between cefaclox and HSA is hydrophobic interaction. The antibiotic valence is related to the transfer efficiency and dissociation constant.
Key concepts: Chemistry, Human serum albumin, Dissociation constant, Fluorescence, Dissociation (chemistry), Aqueous solution, Serum albumin, Photochemistry