Volume 13 Issue 3
Jun.  2020
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ZHANG Hong-cai, LIU Bao-sheng, CHENG Xu. Study on the binding mechanism of cefoxitin sodium to lysozyme by synchronous fluorescence spectroscopy[J]. Chinese Optics, 2020, 13(3): 492-500. doi: 10.3788/CO.2019-0112
Citation: ZHANG Hong-cai, LIU Bao-sheng, CHENG Xu. Study on the binding mechanism of cefoxitin sodium to lysozyme by synchronous fluorescence spectroscopy[J]. Chinese Optics, 2020, 13(3): 492-500. doi: 10.3788/CO.2019-0112

Study on the binding mechanism of cefoxitin sodium to lysozyme by synchronous fluorescence spectroscopy

doi: 10.3788/CO.2019-0112
Funds:  Supported by National Natural Science Foundation of China (No. 21375032)
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  • Corresponding author: lbs@hbu.edu.cn
  • Received Date: 23 Jul 2019
  • Rev Recd Date: 20 Aug 2019
  • Publish Date: 01 Jun 2020
  • Under simulated physiological conditions (pH=7.40), the interaction between tyrosine (Tyr) residue and tryptophan (Trp) residue in lysozyme (LYSO) and cefoxitin sodium (CFXS) was studied using synchronous fluorescence spectroscopy. The results showed that CFXS quenched the fluorescence of Tyr and Trp residue in LYSO by static quenching, and that the number of binding sites n was nearly 1. At 310 K, the fluorescence quenching ratio of CFXS with Trp residue NSFQR(Trp)(60.25%) was higher than that of NSFQR(Tyr)(39.75%), indicating that the binding position was closer to the Trp residue. The Hill coefficient nH was about 1, indicating that the binding of CFXS to the Tyr and Trp residues in LYSO did not affect the binding of subsequent ligands to proteins. The drug binding rate of CFXS to Tyr residue in LYSO was 0.19% to 0.13%, and the drug′s binding rate to Trp residue was 0.23% to 0.14%, respectively. The content of the free drug was almost unchanged. The results showed that the combination of Tyr and Trp residue in LYSO and CFXS did not affect the efficacy of the drug. The protein binding rate of Tyr residue was 52.69% to 54.67%, and the protein binding rate of Trp residue was 67.67% to 69.39%, implying the amount of free amino acid residue in the protein decreased significantly. The main force of the CFXS-LYSO binding system was a hydrophobic interaction. The results of molecular docking showed that there was still a hydrogen bond between the CFXS and LYSO, and the best binding position was near to the active center of the LYSO. The combination of the two substances changed the microenvironment for the amino acid residue at the active center.

     

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