Guan Xiao, Liu Jing, Yin Ting, Li Jing-jun, Liao Li-li
Guang Pu Xue Yu Guang Pu Fen Xi. 2016 Jan;36(1):163-8.
In order to clarify the interaction mechanism of the formation of the resveratrol-hordein nanoparticle, the fluorescence, UV-Vis spectroscopic, FTIR and DSC were used to study the binding reaction between resveratrol and hordein. The fluorescent emission of hordein was inhibited by resveratrol in a dose dependent manner. Fluorescence spectroscopy and DSC indicated that resveratrol interacted with hordein and formed a new complex by a static process. The binding constant (K(A(298 K)) = 2.21 x 10(5) L x mol(-1), K(A(310 K)) =1.53 x 10(4) L x mol(-1)) and the number of binding sites ((n298 K) = 1.23, (n310 K) 0.94) were calculated based on the quenching effect of resveratrol on hordein. Thermodynamic parameter and FTIR indicated that the interaction force between resveratrol and hordein was mainly hydrogen binding and van der Waals force. The binding distance (r0 = 3. 25 nm) between resveratrol and hordein and the energy transfer efficiency (E = 0.227) were obtained according to non-radiative energy transfer theory. The effect of resveratrol on the conformation of hordein was further analyzed by using synchronous fluorescence spectrometry. The results indicated that resveratrol changed the hydrophobicity of tryptophan residue, which caused an obvious influence on the conformation of hordein.
为了阐明白藜芦醇 - 大麦醇溶蛋白纳米颗粒形成的相互作用机制,采用荧光光谱、紫外 - 可见光谱、傅里叶变换红外光谱(FTIR)和差示扫描量热法(DSC)研究白藜芦醇与大麦醇溶蛋白之间的结合反应。白藜芦醇以剂量依赖性方式抑制大麦醇溶蛋白的荧光发射。荧光光谱和DSC表明,白藜芦醇与大麦醇溶蛋白相互作用并通过静态过程形成新的复合物。基于白藜芦醇对大麦醇溶蛋白的猝灭效应计算出结合常数(K(A(298 K)) = 2.21 x 10(5) L x mol(-1),K(A(310 K)) =1.53 x 10(4) L x mol(-1))和结合位点数((n298 K) = 1.23,(n310 K) 0.94)。热力学参数和FTIR表明,白藜芦醇与大麦醇溶蛋白之间的相互作用力主要是氢键和范德华力。根据非辐射能量转移理论获得白藜芦醇与大麦醇溶蛋白之间的结合距离(r0 = 3. 25 nm)和能量转移效率(E = 0.227)。利用同步荧光光谱法进一步分析白藜芦醇对大麦醇溶蛋白构象的影响。结果表明,白藜芦醇改变了色氨酸残基的疏水性,这对大麦醇溶蛋白的构象产生了明显影响。