Polyphenols has attained pronounced attention due to their beneficial values of health and found to prevent several chronic diseases. Here, we elucidated binding mechanism between frequently consumed polyphenol “tea catechin” and milk protein bovine beta-lactoglobulin (β-Lg). We investigated the conformational changes of β-Lg due to interaction with catechin using spectroscopic and in silico studies. Fluorescence quenching data (Stern-Volmer quenching constant) revealed that β-Lg interacted with catechin via dynamic quenching. Thermodynamic data revealed that the interaction between β-Lg and catechin is endothermic and spontaneously interacted mainly through hydrophobic interactions. The UV-Vis absorption and far-UV circular dichroism (CD) spectroscopy exhibited that the tertiary as well as secondary structure of β-Lg distorted after interaction with catechin. Molecular docking and simulation studies also confirm that catechin binds at the central cavity of β-Lg with high affinity (~10⁵ M⁻¹) and hydrophobic interactions play significant role in the formation of a stable β-Lg-catechin complex.

多酚由于其有益于健康的价值而受到了广泛关注，并被发现可以预防多种慢性疾病。在这里，我们阐明了经常食用的多酚“茶儿茶素”与牛奶蛋白牛β-乳球蛋白（β-Lg）之间的结合机制。我们使用光谱和计算机研究研究了由于与儿茶素相互作用而导致的β-Lg构象变化。荧光猝灭数据（Stern-Volmer猝灭常数）表明，β-Lg通过动态猝灭与儿茶素相互作用。热力学数据表明，β-Lg和儿茶素之间的相互作用是吸热的，并且主要通过疏水相互作用自发地相互作用。UV-Vis吸收和远紫外圆二色性（CD）光谱显示，与儿茶素相互作用后，β-Lg的三级和二级结构变形。分子对接和模拟研究还证实了儿茶素以高亲和力（〜10）与β-Lg的中央腔结合⁵ M ^-1）和疏水性相互作用在稳定的β-Lg-儿茶素复合物的形成中起重要作用。