【摘要】 为探究氯霉素与胰蛋白酶的相互作用机制，研究氯霉素对胰蛋白酶结构和活性的影响，利用多种光谱技术和分子对接技术在模拟生理条件下研究氯霉素（chloramphenicol）与胰蛋白酶（trypsin）的相互作用。结果表明：胰蛋白酶的荧光强度随氯霉素浓度的增加而降低，且荧光动态猝灭常数(K_sv)随温度的升高而降低，说明氯霉素能有效猝灭胰蛋白酶荧光，且猝灭作用机制为静态猝灭。热力学参数研究表明氯霉素与胰蛋白酶间相互作用力是以静电引力为主。圆二色谱和傅里叶变换红外光谱结果均显示胰蛋白酶二级结构发生变化。酶活性测定表明，在研究的浓度范围内，氯霉素引起胰蛋白酶活性下降。分子对接结果显示氯霉素可与胰蛋白酶中HIS-57、TYR-59、SER-195形成氢键，进一步表明氯霉素存在对胰蛋白酶结构的影响。综上，氯霉素与胰蛋白酶会发生相互作用，且会对胰蛋白酶的结构和活性产生影响，这为抗生素类药物与体内消化酶的相互作用研究提供可靠的参考依据。更多还原

【Abstract】 In order to explore the interaction mechanism between chloramphenicol and trypsin, and to study the influence of chloramphenicol on the structure and activity of trypsin, this paper studied the interaction between chloramphenicol and trypsin under simulated physiological conditions by using multispectral and molecular docking. The results showed that the fluorescence intensity of trypsin decreased with the increase of chloramphenicol concentration. The fluorescence dynamic quenching constants(K_sv) decreased with the increase of temperature, indicating that chloramphenicol could effectively quenching the fluorescence of trypsin, and chloramphenicol quenched the fluorescence of trypsin through a static process. The thermodynamic parameters showed that the interaction force between chloramphenicol and trypsin was dominated by the electrostatic attraction model. Circular dichroism（CD） and Fourier transform infrared（FTIR） spectroscopy showed that chloramphenicol changed the secondary structure of trypsin. Enzyme activity studies showed that chloramphenicol caused a decrease in trypsin activity in the range of studied concentrations. Molecular docking showed that chloramphenicol can form hydrogen bonds with trypsin HIS-57, TYR-59 and SER-195, respectively. The results showed further evidence that the presence of chloramphenicol affects the structure of trypsin. In summary, chloramphenicol can interact with trypsin and affect the structure and activity of trypsin. This finding can serve as a solid foundation for future research into the in vivo interactions between antibiotic medications and digestive enzymes.更多还原