黄曲霉毒素B1完全抗原构建中结合位点研究

通过衍生化反应,合成了AFB1羧甲基活化物,然后利用碳二亚胺法合成AFB1-O-BSA偶联物,构建AFB1完全抗原,并通过多种光谱和质谱对合成完全抗原过程中偶联比和结合位点进行研究。通过荧光光谱在分子水平上探讨AFB1与BSA载体蛋白的偶联机制及偶联反应对BSA的构象影响,推测黄曲霉毒素和牛血清白蛋白反应的结合部位,同时发生在BSA的酪氨酸残基和色氨酸残基上,使得BSA疏水性增加,肽链伸展程度降低。

Study on the Binding Site in the Construction of AFB1 Complete Antigen

To study the coupling ratio and the binding site of AFB1 and BSA during the construction of the AFB1 complete antigen, AFB1-carboxymethyl and AFB1-O-BSA complexation were synthesized by carbondiimide method. Different kind of spectroscopy and mass spectra methods was employed. The mechanism of the coupling and the effects to the structure of the BSA were investigated in the molecular level. The results showed that the binding sites of the AFB1 and BSA were both situated in the Tyr and Trp residue of the BSA. The binding made the increasing of the hydrophobicity of the BSA and the decreasing of the extension of the peptide chain.