^1HNMR研究苯甲酸钠、维生素C及葡萄糖与蛋白质的结合部位

Study on Interacting Segments of Sodium Benzoate,Vitamin C and Glucose with Proteins by^1HNMR

用1HNMR波谱法研究了苯甲酸钠(SB)、维生素C(VC)及葡萄糖(Glu)分别与牛血清白蛋白(BSA)、胃蛋白酶(Pepsin)结合的主要部位。结果表明,SB与BSA、Pepsin的结合部位为SB分子中的苯环片段,除静电相互作用外,主要以芳香环间π-π电子堆积作用方式相互结合。VC与BSA、Pepsin的结合部位为VC分子结构的乙二醇支链片段,而葡萄糖则以整个分子与BSA、Pepsin结合;VC、葡萄糖主要以分子间氢键方式与蛋白质结合。3种物质分子与BSA和Pepsin结合部位H原子的化学位移改变幅度不大,推测3种物质分子在蛋白质分子上的结合部位可能处于临近蛋白质分子表面的亲水区域层。

The interacting segments of sodium benzoate（SB）,vitamin C（VC） and glucose with bovine serum albumin（BSA）,pepsin,were investigated by means of 1HNMR.Experimental results showed that,the interacting segment of SB was its aromatic ring;besides the electrostatic interaction,the π-π electron interaction existed between the phenyl-ring of SB and aromatic rings of proteins.The interacting segment of VC was its glycol side-chain,and the interacting segment of glucose was its whole molecule.Both VC and glucose bound to proteins through intermolecular hydrogen bond.The slight changes of chemical shifts of H atoms indicated that,the locations of SB,VC and glucose with BSA or pepsin might be the hydrophilic region which was close to protein surface.