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采用荧光光谱、紫外吸收光谱和圆二色谱(CD)研究了聚乙二醇200基硝苯柳胺与钥孔戚血蓝蛋白(KLH)的相互作用。结果表明,聚乙二醇200基硝苯柳胺对KLH的荧光猝灭机制属于静态猝灭;由Lineweaver-Burk方程计算出不同温度下结合常数K,由Van’t Hoff方程计算出△H和△S平均值,结合力主要为静电作用力;根据F rster非辐射能量转移机制求得给体与受体间的结合距离r=5.76 nm;同步荧光光谱表明,聚乙二醇200基硝苯柳胺能够被KLH存储和转运,但结合时对蛋白的构象有一定的影响;圆二色光谱的数据表明相互作用后KLH的二级结构发生了改变:KLH的α-螺旋的含量从43.1%下降到37.8%。
The interaction between PEG-200 and the keyhole limpet hemocyanin (KLH) was investigated by fluorescence spectroscopy, UV absorption spectroscopy and circular dichroism (CD). The results showed that the quenching mechanism of KLH by polyethylene glycol 200-base nisanquat belongs to static quenching. The binding constants K at different temperatures were calculated by Lineweaver-Burk equation and △ H was calculated by the Van’t Hoff equation △ S average, the binding force is mainly electrostatic force; According to F rster non-radiative energy transfer mechanism to obtain donor and acceptor binding distance r = 5.76 nm; Synchronous fluorescence spectra show that polyethylene glycol 200-based nitrobenzene Diphenylamine can be stored and transported by KLH, but the binding has a certain effect on the conformation of the protein. The data of circular dichroism shows that the secondary structure of KLH changes after interaction: the content of a-helix of KLH changes from 43.1% Dropped to 37.8%.