Department of Chemistry, University of Isfahan, Isfahan 81746-73441, Iran.
Department of Chemistry, University of Isfahan, Isfahan 81746-73441, Iran.
Biophys Chem. 2014 Mar-Apr;187-188:33-42. doi: 10.1016/j.bpc.2014.01.003. Epub 2014 Jan 28.
In the present study, the binding properties of naringenin (NG) to β-lactoglobulin (BLG) were explored using spectrofluorimetric and molecular modeling techniques. Analysis of spectrofluorimetric titration data represented the formation of 1:1 complex, significant binding affinity, negative values of entropy and enthalpy changes and the essential role of hydrogen bonding and van der Waals interactions in binding of NG to BLG. The value of determined Förster's distance represents the static mechanism for quenching of BLG by NG. The results of fluorescence competitive binding experiments characterize the location of NG binding site in the outer surface of BLG. Molecular docking study showed that NG binds in the outer surface site of BLG which is accompanied with three hydrogen bonds. The support of molecular docking results by biochemical fluorescence experiments confirms the validity of docking calculation. Analysis of molecular dynamics results indicated that NG can interact with BLG without affecting the secondary structure of protein.
在本研究中，使用荧光光谱法和分子建模技术研究了柚皮素（NG）与β-乳球蛋白（BLG）的结合特性。荧光滴定数据分析表明，形成了 1:1 的复合物，具有显著的结合亲和力，熵和焓变的负值，以及氢键和范德华相互作用在 NG 与 BLG 结合中的重要作用。确定的Förster 距离值代表了 NG 猝灭 BLG 的静态机制。荧光竞争结合实验的结果表征了 NG 在 BLG 外表面的结合部位。分子对接研究表明，NG 结合在 BLG 的外表面结合部位，同时形成三个氢键。生化荧光实验对分子对接结果的支持证实了对接计算的有效性。分子动力学分析结果表明，NG 可以与 BLG 相互作用而不影响蛋白质的二级结构。
