Elucidation of the Binding Mechanisms of Cobalt Phthalocyanine in Serum Albumins: A Computational Modeling Approach and Multispectral

IF 0.7 4区化学 Q4 CHEMISTRY, PHYSICAL

Russian Journal of Physical Chemistry A Pub Date : 2026-10-05 DOI:10.1134/S0036024426602776

Hamid Dezhampanah, Athena Maboodi Haghighi, Hadi Fallah Moafi

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Abstract

The interactions between human and bovine serum albumins (HSA and BSA) as drug carriers and sodium cobalt tetrasulfophthalocyanine (CoTSPc) were examined in this study via a combination of fluorescence, ultraviolet (UV) spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, and molecular docking. Analysis of the fluorescence quenching data revealed a single binding site on both proteins for CoTSPc, with binding constant (K_b) values equal to (3.87 ± 0.15) × 10⁵ for human and (1.41 ± 0.11) × 10⁵ for bovine serum albumin at 298.2 K. The data from synchronous fluorescence and spectroscopic methods, including FT-IR and UV spectroscopy, revealed that the microenvironment and structure of serum albumins, which interact with CoTSPc molecules, changed. Additionally, docking studies suggested that CoTSPc likely binds to subdomain IIIA of HSA/BSA protein molecules, which contain tryptophan residues. Hydrophobic and hydrogen bonding forces are essential for the stability of CoTSPc-protein complexes, depending on the types of amino acid residues that surround CoTSPc molecules.

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酞菁钴在血清白蛋白中的结合机制：一种计算建模方法和多光谱

采用荧光光谱、紫外光谱、傅里叶变换红外光谱和分子对接等方法，研究了作为药物载体的人与牛血清白蛋白（HSA）和牛血清白蛋白（BSA）与CoTSPc的相互作用。荧光猝灭数据分析显示，CoTSPc在两种蛋白上都有一个单一的结合位点，在298.2 K下，人CoTSPc的结合常数（Kb）为（3.87±0.15）× 105，牛血清白蛋白CoTSPc的结合常数（Kb）为（1.41±0.11）× 105。同步荧光和光谱方法（包括FT-IR和UV）的数据显示，与CoTSPc分子相互作用的血清白蛋白的微环境和结构发生了变化。此外，对接研究表明，CoTSPc可能与HSA/BSA蛋白分子的IIIA亚结构域结合，其中含有色氨酸残基。疏水和氢键力对CoTSPc-蛋白复合物的稳定性至关重要，这取决于CoTSPc分子周围氨基酸残基的类型。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Russian Journal of Physical Chemistry A 化学-物理化学

CiteScore

1.20

自引率

14.30%

发文量

376

审稿时长

5.1 months

期刊介绍： Russian Journal of Physical Chemistry A. Focus on Chemistry (Zhurnal Fizicheskoi Khimii), founded in 1930, offers a comprehensive review of theoretical and experimental research from the Russian Academy of Sciences, leading research and academic centers from Russia and from all over the world. Articles are devoted to chemical thermodynamics and thermochemistry, biophysical chemistry, photochemistry and magnetochemistry, materials structure, quantum chemistry, physical chemistry of nanomaterials and solutions, surface phenomena and adsorption, and methods and techniques of physicochemical studies.