胶乳微球与抗体蛋白相互作用机理的荧光光谱法分析

利用共价偶联的方法制备了胶乳-抗体蛋白复合物,并采用荧光光谱法对复合物的性质进行了研究,以揭示胶乳微球与抗体蛋白之间的相互作用机理。内源荧光光谱分析结果表明,共价偶联后,抗体蛋白的最大发射峰发生显著蓝移,最大发射峰强度显著降低,抗体蛋白的三级结构发生了一定的变化,胶乳微球与抗体蛋白之间的相互作用对抗体蛋白的内源荧光有显著的猝灭作用,猝灭效果随着偶联体系pH值以及胶乳浓度的增加而增强,猝灭机制为静态猝灭。外源荧光光谱分析结果表明,共价偶联后抗体蛋白的最大发射峰强度显著增强,且随着偶联体系pH值的升高,抗体蛋白的疏水性显著降低,随着胶乳浓度的增加,疏水性逐渐升高。

Interaction between Latex Microspheres and Antibody Proteins Revealed by Fluorescence Spectroscopy

Latex-antibody complexes were prepared by the method of covalent coupling and the properties of the complexes were studied by fluorescence spectrophotometric method for the purpose of revealing the interaction between latex microspheres and antibody proteins.Analysis of intrinsic fluorescence spectra showed that after being coupled with latex microspheres,the emission maximum of antibody protein showed an obvious blue shift,the intensity of emission maximum decreased significantly,the tertiary structure of antibody protein changed to some extent,the interaction between latex microspheres and antibody proteins had a great quenching effect on the intrinsic fluorescence spectra of antibody proteins,the quenching effect was enhanced along with the increasing pH value and latex concentration,and the quenching mechanism was static quenching.Results of exogenous fluorescence spectra showed that the fluorescence intensity of emission maximum was enhanced significantly after being coupled with latex microspheres,the hydrophobicity of antibody protein was decreasing with the increase in the pH values,however,due to the increasing latex concentration,the hydrophobicity antibody protein was increasing.