State Key Laboratory of Food Science and Technology, Nanchang University, No. 235, Nanjing East Road, Nanchang 330047, China.
State Key Laboratory of Food Science and Technology, Nanchang University, No. 235, Nanjing East Road, Nanchang 330047, China.
Spectrochim Acta A Mol Biomol Spectrosc. 2018 Aug 5;201:197-206. doi: 10.1016/j.saa.2018.05.011. Epub 2018 May 4.
Four kinds of flavonoids (apigenin, naringenin, kaempferol, genistein) were skillfully selected to investigate the interaction between flavonoids and β-lactoglobulin (β-LG) by multi-spectroscopy analysis and molecular docking. Hydrogenation on C2C3 double bond weakened the affinity of apigenin for β-LG and it's most obvious, followed by hydroxylation of C3 and position isomerism of phenyl ring B. The main interaction force for apigenin and naringenin binding to β-LG (van der Waals forces and hydrogen bonds) was different from that of genistein and kaempferol (hydrophobic interactions). Circular dichroism and fluorescence experiments indicated that conformation of β-LG became loose and surface hydrophobicity of β-LG was reduced in the presence of flavonoids. Molecular docking indicated that flavonoids interacted with specific amino acid residues located on the outer surface of β-LG. These findings can provide a deep understanding about the interaction mechanism between flavonoids and protein, and it may be valuable in dairy incorporation with flavonoids.
四种类黄酮（芹菜素、柚皮素、山柰酚、染料木黄酮）被巧妙地选择用于通过多光谱分析和分子对接研究类黄酮与β-乳球蛋白（β-LG）之间的相互作用。C2C3 双键加氢削弱了芹菜素与 β-LG 的亲和力，这是最明显的，其次是 C3 羟基化和苯环 B 的位置异构化。芹菜素和柚皮素与 β-LG（范德华力和氢键）结合的主要相互作用力与染料木黄酮和山柰酚（疏水相互作用力）不同。圆二色性和荧光实验表明，在类黄酮存在的情况下，β-LG 的构象变得松散，β-LG 的表面疏水性降低。分子对接表明，类黄酮与位于β-LG 外表面的特定氨基酸残基相互作用。这些发现可以深入了解类黄酮与蛋白质之间的相互作用机制，对于将类黄酮掺入乳制品中可能具有重要价值。
