Aneja Babita, Kumari Meena, Azam Amir, Kumar Amit, Abid Mohammad, Patel Rajan
Medicinal Chemistry Laboratory, Department of Biosciences, Jamia Millia Islamia, New Delhi, India.
Biophysical Chemistry Laboratory, Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia (A Central University), Jamia Nagar, New Delhi, India.
Luminescence. 2018 May;33(3):464-474. doi: 10.1002/bio.3435. Epub 2018 Jan 5.
The effect of a potent antimicrobial compound bearing 1,2,3-triazole core and a tryptophan tail, triazole-tryptophan hybrid (TTH), with bovine serum albumin (BSA) have been explored using various spectroscopic and molecular docking methods. Studies revealed that TTH strongly quenches the intrinsic fluorophore of BSA by a static quenching mechanism. Time-resolved fluorescence spectra further confirmed the involvement of static quenching for TTH-BSA system. The calculated thermodynamic parameters; ΔH, ΔS, and ΔG showed that the binding process was spontaneous, exothermic and entropy driven. Synchronous fluorescence, three-dimensional (3D) fluorescence and circular dichroism data revealed that TTH induces the structural alteration in BSA and enhances its stability. In silico study of TTH-BSA system showed that it binds with BSA at the site I of subdomain IIA. Both the experimental and in silico study showed that the hydrophobic and electrostatic interactions play a major role in TTH-BSA binding.
使用各种光谱学和分子对接方法，研究了一种带有1,2,3-三唑核心和色氨酸尾的强效抗菌化合物——三唑-色氨酸杂化物（TTH）与牛血清白蛋白（BSA）的相互作用。研究表明，TTH通过静态猝灭机制强烈猝灭BSA的内在荧光团。时间分辨荧光光谱进一步证实了TTH-BSA体系中存在静态猝灭。计算得到的热力学参数ΔH、ΔS和ΔG表明，结合过程是自发的、放热的且由熵驱动。同步荧光、三维（3D）荧光和圆二色性数据表明，TTH诱导了BSA的结构改变并增强了其稳定性。TTH-BSA体系的计算机模拟研究表明，它在亚结构域IIA的位点I与BSA结合。实验和计算机模拟研究均表明，疏水相互作用和静电相互作用在TTH与BSA的结合中起主要作用。
