Molecular insights into binding mechanism of rutin to bovine serum albumin – Levothyroxine complex: Spectroscopic and molecular docking approaches

IF 4.6 2区化学 Q1 SPECTROSCOPY Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy Pub Date : 2022-01-05 DOI:10.1016/j.saa.2021.120261

Nicoleta Sandu , Claudia G. Chilom , Monica Florescu

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引用次数: 10

Abstract

Bovine serum albumin (BSA) has been used as a transporter protein for levothyroxine (LT4) and rutin, due to its property of binding to various ligands. Rutin binding to the BSA-LT4 complex can bring many benefits due to its proven pharmacological properties. Using Fourier-Transform Infrared Spectroscopy (FT-IR) the changes induced by rutin in the structure of BSA-LT4 complex were determined. Fluorescence studies allowed us to determine the quenching mechanism and affinity of rutin to the BSA-LT4 complex. The thermodynamic parameters suggest the binding of rutin to BSA-LT4 is a spontaneous process, driven by enthalpy and electrostatic forces. Also, the second derivative of the emission spectra suggests the Trp’s of BSA are located in two different microenvironments. Thermal and chemical denaturation of BSA-LT4-rutin complex presents similar behavior but with better stability of the complex in case of chemical denaturation. Molecular docking studies show the binding of the two ligands to the same BSA site, suggesting that rutin may influence the bond of LT4 with the protein. Studies on the antioxidant activity of the BSA-LT4-rutin complex suggest that the presence of LT4 decreases the antioxidant activity of the rutin, but even so this antioxidant activity can be used to bring benefits for medical purposes.

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芦丁与牛血清白蛋白-左甲状腺素复合物结合机制的分子观察:光谱和分子对接方法

牛血清白蛋白(BSA)由于能与多种配体结合而被用作左旋甲状腺素(LT4)和芦丁的转运蛋白。芦丁结合BSA-LT4复合体可以带来许多好处，由于其已证实的药理特性。利用傅里叶变换红外光谱(FT-IR)测定了芦丁对BSA-LT4配合物结构的影响。荧光研究使我们能够确定芦丁对BSA-LT4复合物的猝灭机制和亲和力。热力学参数表明芦丁与BSA-LT4的结合是一个自发过程，由焓和静电力驱动。此外，发射光谱的二阶导数表明，BSA的色氨酸位于两个不同的微环境中。bsa - lt4 -芦丁配合物的热变性和化学变性表现出相似的行为，但在化学变性情况下配合物的稳定性更好。分子对接研究表明，这两个配体结合在同一个BSA位点上，这表明芦丁可能影响LT4与蛋白质的结合。对bsa -LT4-芦丁复合物抗氧化活性的研究表明，LT4的存在降低了芦丁的抗氧化活性，但即使如此，这种抗氧化活性也可以用于医疗目的。

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来源期刊

Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 物理-光谱学

CiteScore

8.40

自引率

11.40%

发文量

1364

审稿时长

40 days

期刊介绍： Spectrochimica Acta, Part A: Molecular and Biomolecular Spectroscopy (SAA) is an interdisciplinary journal which spans from basic to applied aspects of optical spectroscopy in chemistry, medicine, biology, and materials science. The journal publishes original scientific papers that feature high-quality spectroscopic data and analysis. From the broad range of optical spectroscopies, the emphasis is on electronic, vibrational or rotational spectra of molecules, rather than on spectroscopy based on magnetic moments. Criteria for publication in SAA are novelty, uniqueness, and outstanding quality. Routine applications of spectroscopic techniques and computational methods are not appropriate. Topics of particular interest of Spectrochimica Acta Part A include, but are not limited to: Spectroscopy and dynamics of bioanalytical, biomedical, environmental, and atmospheric sciences, Novel experimental techniques or instrumentation for molecular spectroscopy, Novel theoretical and computational methods, Novel applications in photochemistry and photobiology, Novel interpretational approaches as well as advances in data analysis based on electronic or vibrational spectroscopy.