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Domain-Specific Association of a Phenanthrene–Pyrene-Based Synthetic Fluorescent Probe with Bovine Serum Albumin: Spectroscopic and Molecular Docking Analysis
ACS Omega ( IF 3.7 ) Pub Date : 2018-06-12 00:00:00 , DOI: 10.1021/acsomega.8b00186 Mihir Sasmal 1 , Rahul Bhowmick 1 , Abu Saleh Musha Islam 1 , Sutanwi Bhuiya 1 , Suman Das 1 , Mahammad Ali 1
ACS Omega ( IF 3.7 ) Pub Date : 2018-06-12 00:00:00 , DOI: 10.1021/acsomega.8b00186 Mihir Sasmal 1 , Rahul Bhowmick 1 , Abu Saleh Musha Islam 1 , Sutanwi Bhuiya 1 , Suman Das 1 , Mahammad Ali 1
Affiliation
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In this report, the interaction between a phenanthrene–pyrene-based fluorescent probe (PPI) and bovine serum albumin (BSA), a transport protein, has been explored by steady-state emission spectroscopy, fluorescence anisotropy, far-ultraviolet circular dichroism (CD), time-resolved spectral measurements, and molecular docking simulation study. The blue shift along with emission enhancement indicates the interaction between PPI and BSA. The binding of the probe causes quenching of BSA fluorescence through both static and dynamic quenching mechanisms, revealing a 1:1 interaction, as delineated from Benesi–Hildebrand plot, with a binding constant of ∼105 M–1, which is in excellent agreement with the binding constant extracted from fluorescence anisotropy measurements. The thermodynamic parameters, ΔH°, ΔS°, and ΔG°, as determined from van’t Hoff relationship indicate the predominance of van der Waals/extensive hydrogen-bonding interactions for the binding phenomenon. The molecular docking and site-selective binding studies reveal the predominant binding of PPI in subdomain IIA of BSA. From the fluorescence resonance energy transfer study, the average distance between tryptophan 213 of the BSA donor and the PPI acceptor is found to be 3.04 nm. CD study demonstrates the reduction of α-helical content of BSA protein on binding with PPI, clearly indicating the change of conformation of BSA.
中文翻译：
菲-P合成荧光探针与牛血清白蛋白的领域特定关联：光谱和分子对接分析
在本报告中，已通过稳态发射光谱，荧光各向异性，远紫外线圆二色性（CD）探索了基于菲py的荧光探针（PPI）和牛血清白蛋白（BSA）之间的相互作用，而牛血清白蛋白是一种转运蛋白。 ），时间分辨光谱测量和分子对接模拟研究。蓝移和发射增强指示PPI和BSA之间的相互作用。探针的结合通过静态和动态淬灭机制引起BSA荧光的淬灭，显示1：1相互作用，如Benesi–Hildebrand图所描绘，结合常数约为10 5 M –1，这与从荧光各向异性测量中提取的结合常数非常吻合。由van't Hoff关系确定的热力学参数ΔH °，ΔS °和ΔG °表示范德华/广泛的氢键相互作用对于结合现象的优势。分子对接和位点选择性结合研究揭示了PSA在BSA的IIA亚域中的主要结合。根据荧光共振能量转移研究，发现BSA供体的色氨酸213与PPI受体之间的平均距离为3.04 nm。CD研究表明，与PPI结合后，BSA蛋白的α-螺旋含量降低，清楚地表明了BSA构象的变化。
更新日期：2018-06-12
中文翻译：
菲-P合成荧光探针与牛血清白蛋白的领域特定关联：光谱和分子对接分析
在本报告中，已通过稳态发射光谱，荧光各向异性，远紫外线圆二色性（CD）探索了基于菲py的荧光探针（PPI）和牛血清白蛋白（BSA）之间的相互作用，而牛血清白蛋白是一种转运蛋白。 ），时间分辨光谱测量和分子对接模拟研究。蓝移和发射增强指示PPI和BSA之间的相互作用。探针的结合通过静态和动态淬灭机制引起BSA荧光的淬灭，显示1：1相互作用，如Benesi–Hildebrand图所描绘，结合常数约为10 5 M –1，这与从荧光各向异性测量中提取的结合常数非常吻合。由van't Hoff关系确定的热力学参数ΔH °，ΔS °和ΔG °表示范德华/广泛的氢键相互作用对于结合现象的优势。分子对接和位点选择性结合研究揭示了PSA在BSA的IIA亚域中的主要结合。根据荧光共振能量转移研究，发现BSA供体的色氨酸213与PPI受体之间的平均距离为3.04 nm。CD研究表明，与PPI结合后，BSA蛋白的α-螺旋含量降低，清楚地表明了BSA构象的变化。
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