a Department of Chemistry , Jadavpur University , Kolkata 700 032 , India.
b Department of Chemistry , Kalyani University , Kalyani 741235 , India.
J Biomol Struct Dyn. 2018 Nov;36(14):3773-3790. doi: 10.1080/07391102.2017.1400468. Epub 2017 Nov 20.
The interaction between a synthesized dye with proteins, bovine, and human serum albumin (BSA, HSA, respectively) under physiological conditions has been characterized in detail, by means of steady-state and time-resolved fluorescence, UV-vis absorption, and circular dichroism (CD) techniques. An extensive time-resolved fluorescence spectroscopic characterization of the quenching process has been undertaken in conjugation with temperature-dependent fluorescence quenching studies to divulge the actual quenching mechanism. From the thermodynamic observations, it is clear that the binding process is a spontaneous molecular interaction, in which van der Waals and hydrogen bonding interactions play the major roles. The UV-vis absorption and CD results confirm that the dye can induce conformational and micro-environmental changes of both the proteins. In addition, the dye binding provokes the functionality of the native proteins in terms of esterase-like activity. The average binding distance (r) between proteins and dye has been calculated using FRET. Cytotoxicity and antiviral effects of the dye have been found using Vero cell and HSV-1F virus by performing MTT assay. The AutoDock-based docking simulation reveals the probable binding location of dye within the sub-domain IIA of HSA and IB of BSA.
在生理条件下，通过稳态和时间分辨荧光、紫外可见吸收和圆二色性 (CD) 技术详细研究了合成染料与蛋白质（牛血清白蛋白 (BSA) 和人血清白蛋白 (HSA)）之间的相互作用。结合温度依赖的荧光猝灭研究，对猝灭过程进行了广泛的时间分辨荧光光谱表征，以揭示实际的猝灭机制。从热力学观察结果可以清楚地看出，结合过程是一种自发的分子相互作用，其中范德华力和氢键相互作用起着主要作用。紫外可见吸收和 CD 结果证实，染料可以诱导两种蛋白质的构象和微环境变化。此外，染料结合会引发天然蛋白质的功能，表现为酯酶样活性。使用 FRET 计算了蛋白质和染料之间的平均结合距离 (r)。通过 MTT 测定法，使用 Vero 细胞和 HSV-1F 病毒研究了染料的细胞毒性和抗病毒作用。基于 AutoDock 的对接模拟揭示了染料在 HSA 的亚结构域 IIA 和 BSA 的亚结构域 IB 内的可能结合位置。
