Advanced Ceramics and Nanotechnology Laboratory, Department of Materials Engineering, University of Concepcion, Concepcion, Chile; Nanomaterials & Solar Energy Conversion Lab, Department of Chemistry, National Institute of Technology, Tiruchirappalli 620015, India.
School of Chemistry, Bharathidasan University, Tiruchirappalli 620024, India.
Spectrochim Acta A Mol Biomol Spectrosc. 2018 Mar 5;192:34-40. doi: 10.1016/j.saa.2017.10.075. Epub 2017 Oct 31.
The interaction of Acid Orange 10 (AO10) with bovine serum albumin (BSA) was investigated comparatively with that of human serum albumin (HSA) using multispectroscopic techniques for understanding their toxic mechanism. Further, density functional theory calculations and docking studies have been carried out to gain more insights into the nature of interactions existing between AO10 and serum albumins. The fluorescence results suggest that AO10 quenched the fluorescence of BSA through the combination of static and dynamic quenching mechanism. The same trend was followed in the interaction of AO10 with HSA. In addition to the type of quenching mechanism, the fluorescence spectroscopic results suggest that the binding occurs near the tryptophan moiety of serum albumins and the binding. AO10 has more binding affinity towards BSA than HSA. An AO10-Trp model has been created to explicitly understand the CHπ interactions from Bader's quantum theory of atoms in molecules analysis which confirmed that AO10 bind more strongly with BSA than that of HSA due to the formation of three hydrogen bonds with BSA whereas it forms two hydrogen bonds in the case of HSA. These obtained results provide an in-depth understanding of the interaction of the acid azo dye AO10 with serum albumins. This interaction study provides insights into the underlying reasons for toxicity of AO10 relevant to understand its effect on bovids and humans during the blood transportation process.
采用多光谱技术比较研究了酸性橙 10（AO10）与人血清白蛋白（HSA）与牛血清白蛋白（BSA）的相互作用，以了解其毒性机制。此外，还进行了密度泛函理论计算和对接研究，以更深入地了解 AO10 与血清白蛋白之间存在的相互作用的性质。荧光结果表明，AO10 通过静态和动态猝灭机制猝灭了 BSA 的荧光。AO10 与 HSA 的相互作用也遵循相同的趋势。除了猝灭机制的类型外，荧光光谱结果表明，结合发生在血清白蛋白的色氨酸部分附近，并且结合。AO10 与 BSA 的结合亲和力大于 HSA。创建了一个 AO10-Trp 模型，以便从分子中的原子的量子理论的 Bader 明确理解 CHπ 相互作用分析，这证实了 AO10 与 BSA 的结合比 HSA 强得多，因为它与 BSA 形成三个氢键，而在 HSA 的情况下形成两个氢键。这些获得的结果提供了对酸性偶氮染料 AO10 与血清白蛋白相互作用的深入了解。该相互作用研究深入了解了 AO10 的毒性的潜在原因，有助于了解其在血液运输过程中对牛和人类的影响。
