Maurya Neha, Maurya Jitendra Kumar, Kumari Meena, Khan Abbul Bashar, Dohare Ravins, Patel Rajan
a Biophysical Chemistry Laboratory, Centre for Interdisciplinary Research in Basic Sciences , Jamia Millia Islamia (A Central University) , New Delhi , India.
b Nonlinear Dynamic Laboratory, Centre for Interdisciplinary Research in Basic Sciences , Jamia Millia Islamia (A Central University) , New Delhi , India.
J Biomol Struct Dyn. 2017 May;35(6):1367-1380. doi: 10.1080/07391102.2016.1184184. Epub 2016 Jun 1.
Herein, we have explored the interaction between amitriptyline hydrochloride (AMT) and hemoglobin (Hb), using steady-state and time-resolved fluorescence spectroscopy, UV-visible spectroscopy, and circular dichroism spectroscopy, in combination with molecular docking and molecular dynamic (MD) simulation methods. The steady-state fluorescence reveals the static quenching mechanism in the interaction system, which was further confirmed by UV-visible and time-resolved fluorescence spectroscopy. The binding constant, number of binding sites, and thermodynamic parameters viz. ΔG, ΔH, ΔS are also considered; result confirms that the binding of the AMT with Hb is a spontaneous process, involving hydrogen bonding and van der Waals interactions with a single binding site, as also confirmed by molecular docking study. Synchronous fluorescence, CD data, and MD simulation results contribute toward understanding the effect of AMT on Hb to interpret the conformational change in Hb upon binding in aqueous solution.
在此，我们运用稳态和时间分辨荧光光谱、紫外可见光谱以及圆二色光谱，并结合分子对接和分子动力学（MD）模拟方法，探究了盐酸阿米替林（AMT）与血红蛋白（Hb）之间的相互作用。稳态荧光揭示了相互作用体系中的静态猝灭机制，紫外可见光谱和时间分辨荧光光谱进一步证实了这一点。还考虑了结合常数、结合位点数以及热力学参数，即ΔG、ΔH、ΔS；结果证实AMT与Hb的结合是一个自发过程，涉及氢键和范德华相互作用，且只有一个结合位点，分子对接研究也证实了这一点。同步荧光、圆二色数据以及分子动力学模拟结果有助于理解AMT对Hb的影响，以解释在水溶液中结合时Hb的构象变化。
