Elucidation on the interaction between ascorbic acid and β-lactoglobulin based on multi-spectroscopic analysis and molecular simulation approach

IF 5.2 2区化学 Q2 CHEMISTRY, PHYSICAL Journal of Molecular Liquids Pub Date : 2025-02-11 DOI:10.1016/j.molliq.2025.127129

Bahareh Yousefi , Saad Ali Alshehri , Sadegh Farhadian , Behzad Shareghi , Taghreed A. Majrashi , Sami Saad Alghamdi , Mohammad Gholizadeh , Akhtar Atiya , Reza Assaran- Darban

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Abstract

The binding mechanism between Ascorbic acid (AscA) and β-lactoglobulin (β-Lg) was thoroughly examined in this study using a variety of techniques, such as multi-spectroscopic analysis, thermodynamic measurements, molecular docking, and MD simulation at pH 7.4. The results indicated that the protein AscA was able to interact with the protein β-Lg, which led to a decrease in the fluorescence intensity of β-Lg. The interaction between AscA and β-Lg resulted in a decrease in the hydrophobicity of the local environment surrounding the tryptophan and tyrosine residues within the β-Lg protein. Additionally, changes in the secondary structure of the β-Lg protein were observed using Circular dichroism (CD), Fourier-transform infrared spectroscopy (FTIR), and simulation techniques. These structural changes were consistent with the calculated Tm analysis, Root means square deviation (RMSD), Radius of Gyration (RG), and solvent-accessible surface area (SASA) parameters. The analysis of fluorescence spectroscopy suggested that the formation of the β-Lg-(AscA) complex relies heavily on hydrogen and van der Waals interactions. The findings from this study offer new insights into the interaction mechanism between the β-Lg and AscA proteins. The results suggest that β-Lg can be utilized as a delivery vehicle for AscA in functional food applications.

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基于多光谱分析和分子模拟的抗坏血酸与β-乳球蛋白相互作用研究

本研究使用多种技术，如多光谱分析、热力学测量、分子对接和pH 7.4下的MD模拟，深入研究了抗坏血酸（AscA）与β-乳球蛋白（β-Lg）的结合机制。结果表明，AscA蛋白能够与β-Lg蛋白相互作用，导致β-Lg的荧光强度降低。AscA与β-Lg之间的相互作用导致β-Lg蛋白内色氨酸和酪氨酸残基周围局部环境的疏水性降低。此外，利用圆二色性（CD）、傅里叶变换红外光谱（FTIR）和模拟技术观察了β-Lg蛋白二级结构的变化。这些结构变化与计算的Tm分析、均方根偏差（RMSD）、旋转半径（RG）和溶剂可及表面积（SASA）参数一致。荧光光谱分析表明，β-Lg-(AscA)配合物的形成很大程度上依赖于氢和范德华相互作用。本研究结果为β-Lg和AscA蛋白之间的相互作用机制提供了新的见解。结果表明，β-Lg可作为AscA在功能食品中的递送载体。

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来源期刊

Journal of Molecular Liquids 化学-物理：原子、分子和化学物理

CiteScore

10.30

自引率

16.70%

发文量

2597

审稿时长

78 days

期刊介绍： The journal includes papers in the following areas: – Simple organic liquids and mixtures – Ionic liquids – Surfactant solutions (including micelles and vesicles) and liquid interfaces – Colloidal solutions and nanoparticles – Thermotropic and lyotropic liquid crystals – Ferrofluids – Water, aqueous solutions and other hydrogen-bonded liquids – Lubricants, polymer solutions and melts – Molten metals and salts – Phase transitions and critical phenomena in liquids and confined fluids – Self assembly in complex liquids.– Biomolecules in solution The emphasis is on the molecular (or microscopic) understanding of particular liquids or liquid systems, especially concerning structure, dynamics and intermolecular forces. The experimental techniques used may include: – Conventional spectroscopy (mid-IR and far-IR, Raman, NMR, etc.) – Non-linear optics and time resolved spectroscopy (psec, fsec, asec, ISRS, etc.) – Light scattering (Rayleigh, Brillouin, PCS, etc.) – Dielectric relaxation – X-ray and neutron scattering and diffraction. Experimental studies, computer simulations (MD or MC) and analytical theory will be considered for publication; papers just reporting experimental results that do not contribute to the understanding of the fundamentals of molecular and ionic liquids will not be accepted. Only papers of a non-routine nature and advancing the field will be considered for publication.