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首页> 外文期刊>RSC Advances >Spectroscopic exploration of drug-protein interaction: a study highlighting the dependence of the magnetic field effect on inter-radical separation distance formed during photoinduced electron transfer
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Spectroscopic exploration of drug-protein interaction: a study highlighting the dependence of the magnetic field effect on inter-radical separation distance formed during photoinduced electron transfer

机译：药物-蛋白质相互作用的光谱探索：一项研究突出了磁场效应对光致电子转移过程中形成的自由基间距的依赖性

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In this article, we study the binding interaction of acridone (AD) with human serum albumin (HSA) using conventional spectroscopic techniques and then decipher the latent occurrence of photoinduced electron transfer (PET) using the laser flash photolysis (LFP) technique in conjunction with a weak magnetic field (MF). The experimental observations are further substantiated by docking results. An absorption study reveals the formation of a ground state complex between AD and HSA while a circular dichroism study implies that AD brings about a substantial change in the secondary and tertiary structures of the protein. A fluorescence study mainly helps in evaluation of the binding and thermodynamic parameters. This is one of the rare reports which utilize time-resolved emission spectra and time-resolved area normalized emission spectra to study drug-protein interactions. The detection of the occurrence of PET would be ignored if only the observations of conventional spectroscopic techniques had been considered. LFP detects the occurrence of PET from the tryptophan residue of HSA to AD and MF effect authenticates the triplet origin of the radical ions involved. Furthermore, the actual reaction pathway is elucidated with the help of the MF effect. Although the MF effect is generally observed in a restricted medium, in the present case the complex structure of the protein offers pseudo-confinement to the radical pairs or radical ion pairs resulting in observation of a substantial MF effect. The significance of maintaining the condition of "pseudo-confinement" or the optimum distance between radical ions originating from the acceptor and donor moieties in the observation of the MF effect has been specifically highlighted in this work by integrating the findings of the present study with our previous reports.
机译：在本文中，我们使用常规的光谱技术研究了d啶酮（AD）与人血清白蛋白（HSA）的结合相互作用，然后使用激光闪光光解（LFP）技术结合使用了破译的光诱导电子转移（PET）的潜在可能性。弱磁场（MF）。对接结果进一步证实了实验观察结果。吸收研究揭示了AD和HSA之间形成了基态复合物，而圆二色性研究表明AD引起了蛋白质二级和三级结构的实质性变化。荧光研究主要有助于评估结合和热力学参数。这是利用时间分辨发射光谱和时间分辨面积归一化发射光谱研究药物-蛋白质相互作用的罕见报告之一。如果仅考虑常规光谱技术的观察结果，则将忽略PET发生的检测。 LFP检测从HSA色氨酸残基到AD的PET的发生，MF效应验证了所涉及的自由基离子的三重态起源。此外，借助MF效应阐明了实际的反应途径。尽管通常在受限的培养基中观察到MF效应，但在目前情况下，蛋白质的复杂结构对自由基对或自由基离子对提供了假限制，导致观察到了明显的MF效应。通过将本研究的发现与我们的研究相结合，在这项工作中特别强调了维持“伪限制”条件或源自受体和供体部分的自由基离子之间最佳距离的重要性。以前的报告。

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