Surfactant Research Chair, Department of Chemistry, College of Science, King Saud University, P.O. Box-2455, Riyadh 11451, Saudi Arabia.
School of Computational and Integrative Science, Jawaharlal Nehru University, New Delhi, India.
Int J Biol Macromol. 2023 Dec 1;252:126568. doi: 10.1016/j.ijbiomac.2023.126568. Epub 2023 Aug 26.
The interaction of lysozyme with cefoperazone was studied by means of spectroscopic and computational approaches. The change in the UV-visible spectrum of lysozyme in presence of cefoperazone was an indication of the complex formation between them. Fluorescence spectroscopy suggested that there was a fair interaction between the protein and drug which was taken place via dynamic quenching mechanism and the binding ratio was approximately 1:1. The binding was energetically feasible and principally supported by the hydrophobic forces. CD spectroscopic studies have shown that cefoperazone induced the secondary structure of lysozyme by increasing the α-helical contents of the latter. In silico studies revealed that the large nonpolar cavity was the preferred binding site of cefoperazone within lysozyme and the interaction was taken place mainly through hydrophobic forces with small involvement of hydrogen bonding and electrostatic interactions which is in good agreement with the experimental analyses. Effect of paracetamol was also seen on the binding and it was found that paracetamol had a negative influence on the binding between cefoperazone and lysozyme.
通过光谱和计算方法研究了溶菌酶与头孢哌酮的相互作用。在头孢哌酮存在下溶菌酶的紫外可见光谱的变化表明它们之间形成了复合物。荧光光谱表明，蛋白质和药物之间存在相当大的相互作用，这是通过动态猝灭机制发生的，结合比约为 1:1。结合在能量上是可行的，主要是由疏水作用力支持的。圆二色性光谱研究表明，头孢哌酮通过增加后者的α-螺旋含量诱导溶菌酶的二级结构。计算机研究表明，大的非极性腔是头孢哌酮在溶菌酶内的首选结合位点，相互作用主要通过疏水作用力发生，氢键和静电相互作用的参与较小，这与实验分析结果一致。对乙酰氨基酚的影响也见于结合，发现对乙酰氨基酚对头孢哌酮与溶菌酶之间的结合有负面影响。
