纳米粒子共存下白藜芦醇与牛血清白蛋白相互作用的光谱研究

Interaction Study of Resveratrol and Bovine Serum Albumin with Nanoparticles by Spectrometry

采用荧光光谱和紫外吸收光谱法,研究了在0.1mol·L-1磷酸缓冲溶液(PBS,p H=7.4)中碳纳米管(CNTs)和金纳米粒子(Au NP)共存时,荧光活性物质白藜芦醇(Res)与牛血清白蛋白(BSA)的相互作用。实验表明:通过荧光光谱的变化,证明了Res与BSA作用形成了配合物,CNTs、Au NP和Res都对BSA具有荧光猝灭效应,根据同步荧光光谱,利用Lineweaver-Burk方程求算CNTs(或Au NP)与Trp/BSA和Res与Trp/BSA(或Tyr/BSA)的结合常数K和配位数n。结果表明:CNTs和Au NP主要与BSA表面附近的Trp残基作用,不与分子内部的Tyr残基作用,但Res可与Trp和Tyr两种残基结合,且Res与Trp的结合比Tyr强。

The interaction between fluorescent active substance resveratrol and bovine serum albumin（ BSA） was studied by using fluorescence spectroscopy and ultraviolet absorbance spectroscopy under the condition of 0. 1 mol · L-1（ PBS,p H = 7. 4） with carbon nanotubes（ CNTs） and gold nanoparticles（ Au NP）.Fluorescence spectrum results showed that Res was able to form complex with BSA.Moreover,the fluorescence of Res and BSA can be quenched by CNTs and Au NP.According to the equation of Lineweaver-Burk,the values of binding constant K and binding site n of CNTs（ Au NP）-Trp/BSA and Res-Tyr/BSA（ Trp/BSA） were calculated.The results showed that CNTs and Au NP mainly interacted with the superficial Trp residues of BSA rather than interacted with the internal Tyr residues.However,Res molecules were able to interact with both Trp and Tyr residues within BSA.It is noted that the binding activity of Res to Trp residue was stronger than that of Res to Tyr residue.