同步荧光光谱探究头孢西丁钠与溶菌酶的结合机制

张红彩; 刘保生; 程旭

doi:10.3788/CO.2019-0112

Volume 13 Issue 3

Jun. 2020

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Chinese Optics > 2020 > 13(3): 492-500.

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

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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

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

doi: 10.3788/CO.2019-0112

ZHANG Hong-cai^{1, 2, 3
,},
LIU Bao-sheng^{1, 2, 3
,
,},
CHENG Xu^{1, 2, 3}

1.
College of Chemistry & Environmental Science, Hebei University, Baoding 071002, China
2.
Key Laboratory of Analytical Science and Technology of Hebei Province, Baoding 071002, China
3.
National Chemistry Experimental Teaching Demonstration Center, Hebei University, Baoding 071002, China

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

Abstract

Abstract

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 N_SFQR(Trp)(60.25%) was higher than that of N_SFQR(Tyr)(39.75%), indicating that the binding position was closer to the Trp residue. The Hill coefficient n_H 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.
- synchronous fluorescence,
- cefoxitin sodium,
- lysozyme,
- fluorescent group,
- molecular docking

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References(32)

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

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