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首页> 外文期刊>Journal of biochemical and molecular toxicology >Determination on the binding of chlortetracycline to bovine serum albumin using spectroscopic methods
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Determination on the binding of chlortetracycline to bovine serum albumin using spectroscopic methods

机译：光谱法测定金霉素与牛血清白蛋白的结合

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摘要

In this work, the interaction of chlortetracycline with bovine serum albumin (BSA) was investigated by fluorescence spectroscopy, circular dichroism (CD) spectroscopy, and molecular docking. Results indicated that chlortetracycline quenches BSA fluorescence mainly by a static quenching mechanism. The quenching constants (K SV) were obtained as 5.64 × 10 4, 4.49 × 10 4/, and 3.44 × 10 4/ M -1 at 283, 295, and 307 K, respectively. The thermodynamic parameters of enthalpy change Δ H°, entropy change Δ S°, and free energy change Δ G° were -5.12 × 10 4/ J mol-1, -97.6 J mol-1 K-1, and -2.24 × 10 4/ J mol-1 (295 K), respectively. The association constant (K A) and the number of binding sites (n) were 9.41 × 10 3/ M-1 and 0.86, respectively. The analysis results suggested that the interaction was spontaneous, and van der Waals force and hydrogen-bonding interactions played key roles in the reaction process. In addition, CD spectra proved secondary structure alteration of BSA in the presence of chlortetracycline.
机译：在这项工作中，通过荧光光谱，圆二色性（CD）光谱和分子对接研究了金霉素与牛血清白蛋白（BSA）的相互作用。结果表明，金霉素主要通过静态猝灭机制猝灭BSA荧光。淬火常数（K SV）在283、295和307 K分别为5.64×10 4、4.49×10 4 /和3.44×10 4 / M -1。焓变ΔH°，熵变ΔS°和自由能变化ΔG°的热力学参数分别为-5.12×10 4 / J mol-1，-97.6 J mol-1 K-1和-2.24×10 4 / J mol-1（295 K）。缔合常数（K A）和结合位点数（n）分别为9.41×10 3 / M-1和0.86。分析结果表明相互作用是自发的，范德华力和氢键相互作用在反应过程中起关键作用。另外，CD光谱证明在金霉素存在下BSA的二级结构改变。

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