Abstract
The binding mechanism between cefetamet pivoxil (CFP) and pepsin (PEP) at different temperatures (298 K, 303 K, 310 K) was investigated by the classical fluorescence spectroscopy with focus on the fluorescence change of protein, as well as the improved spectroscopy with focus on the fluorescence changes of the resonance light scattering of small molecule drugs. The results showed that the main quenching mode of PEP-CFP was static quenching. The value of n was approximately equal to 1 which indicating that there was only one binding site in the interaction between PEP and CFP and the Hill coefficient was about 1 which indicating that there was no cooperative between the receptor PEP and ligand CFP. The binding constants of the PEP-CFP system obtained by the improved spectroscopic method were two orders of magnitude larger than that of the traditional fluorescence spectroscopy, which showed that the study of the small drug molecule was more practical and reasonable. The rationality of the experimental results obtained was verified by ultraviolet absorption spectroscopy.
Highlights
The fluorescence of protein is mainly caused by tryptophan residues and the information of other non-fluorescent amino acid residues interacting with drugs in the protein cannot be reflected in the traditional fluorescence spectrum [1]
The mechanism of action of PEP-CFP system was studied by resonance light scattering method, and the rationality of the experimental results obtained was tested by ultraviolet absorption spectroscopy
Resonance Light Scattering Spectroscopy At 298, 303 and 310 K, 1.0 mL of Tris-HCl buffer, pH=7.40, 1.0 mL of 1.0×10-5 mol·L-1 CFP solution and different volume of PEP solution were added into 10 mL colorimetric tube successively
Summary
The fluorescence of protein is mainly caused by tryptophan residues and the information of other non-fluorescent amino acid residues interacting with drugs in the protein cannot be reflected in the traditional fluorescence spectrum [1]. The spectrum can only reflect part of the information of the interaction between the entire protein molecule and the drug, resulting in inaccurate and one-sided information obtained. A new method by taking the drug as the object of detection was applied to study the interaction between drugs and proteins and the results obtained were more accurate and reliable. Cefetamet pivoxil (Cefetamet pivoxil, referred to as CFP) is the third generation cephalosporin, which antibacterial spectrum is wider than the first and second generation cephalosporin It mainly used in clinical infection caused by a variety of sensitive bacteria, such as ENT, lower respiratory tract, urinary tract, skin and soft tissue [3]. The results showed that compared with the traditional protein, the drug as the test object could express the protein-drug interaction information comprehensively and accurately. Hongcai Zhang et al.: Comparative Studies on the Interaction Between the Medicine Small Molecule with
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