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首页> 外文期刊>Spectrochimica acta, Part A. Molecular and biomolecular spectroscopy >Comparing the binding interaction between beta-lactoglobulin and flavonoids with different structure by multi-spectroscopy analysis and molecular docking
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Comparing the binding interaction between beta-lactoglobulin and flavonoids with different structure by multi-spectroscopy analysis and molecular docking

机译：用多光谱分析和分子对接比较β-乳酰酚蛋白和黄酮类化合物与黄酮类化合物的结合相互作用

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摘要

Four kinds of flavonoids (apigenin, naringenin, kaempferol, genistein) were skillfully selected to investigate the interaction between flavonoids and A-lactoglobulin (beta-LG) by multi-spectroscopy analysis and molecular docking. Hydrogenation on C2=C3 double bond weakened the affinity of apigenin for beta-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 beta-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 beta-LG became loose and surface hydrophobicity of beta-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 beta-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. (C) 2018 Elsevier B.V. All rights reserved.
机译：巧妙地选择四种类黄酮（Apigenin，Naringenin，Kaempferol，Genistein）以通过多光谱分析和分子对接研究黄酮类化合物和α-乳酰脲（Beta-Lg）之间的相互作用。 C2 = C3双键的氢化削弱了Apigenin对β-LG的亲和力，并且最明显，其次是C3的羟基化和苯环的位置异构体。磷酸蛋白和鼻疽蛋白的主要相互作用力与β-LG结合（van der WAALS部队和氢键值不同于Genistein和Kaempferol（疏水相互作用）的不同。圆形二色性和荧光实验表明，在黄酮类化合物存在下，β-Lg的构象变得松弛，并且β-Lg的表面疏水性降低。分子对接表明黄酮类化合物与位于β-LG外表面上的特定氨基酸残基相互作用。这些发现可以对黄酮类化合物和蛋白质之间的相互作用机制提供深刻的理解，并且在乳制品与黄酮类化合物中可能是有价值的。 （c）2018年elestvier b.v.保留所有权利。

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