Abstract：
The binding capacity of β-Lactoglobulin (BLG) is crucial for delivering polyphenols, influenced by structural changes. High pressure processing (HPP) has the potential to modify BLG\'s structure and aggregation, but its specific impact on BLG-polyphenol interactions is uncertain. This study used circular dichroism spectroscopy and molecular dynamics simulations to reveal HPP-induced structural changes in BLG, supported by particle size analysis indicating aggregation. Seven structurally diverse polyphenols (quercetin-QR, hesperetin-HSP, dihydromyricetin-DHM, gallic acid-GA, (-)-epicatechin-EC, resveratrol-RES, and secoisolariciresinol diglucoside-SDG) were investigated to comprehensively analyze their binding patterns using fluorescence spectroscopy and molecular docking. HPP reduced BLG\'s ordered structure and increased its aggregation. Binding affinities peaked at 400 MPa for DHM, QR, HSP, GA, and RES, while SDG and EC exhibited maximum affinities at atmospheric pressure and 600 MPa, respectively. Elevated pressures enhanced BLG-polyphenol interactions, particularly at residues 44GLU and 160CYS, with van der Waals forces dominating the binding free energy.
摘要：
β-乳球蛋白（BLG）的结合能力对于递送多酚至关重要，结构变化的影响。高压处理(HPP)有可能改变BLG的结构和聚集，但其对BLG-多酚相互作用的具体影响尚不确定。这项研究使用圆二色光谱和分子动力学模拟来揭示HPP引起的BLG结构变化，由指示聚集的粒度分析支持。七种结构多样的多酚(槲皮素-QR，Hesperetin-HSP,二氢杨梅素-DHM,没食子酸-GA，(-)-表儿茶素-EC,白藜芦醇-RES，和secoisolariciresinol二糖苷-SDG）进行了研究，以使用荧光光谱和分子对接全面分析其结合模式。HPP减少了BLG的有序结构，增加了其聚集。DHM的结合亲和力峰值为400MPa，QR，HSP,GA,和RES,而SDG和EC在大气压和600MPa下表现出最大亲和力，分别。升高的压力增强了BLG-多酚相互作用，特别是在44GLU和160CYS残基处，范德华力支配着束缚自由能。
