Abstract:

This study aimed to examined the effect of Cu2+ on the structure and allergenicity of TBt, a major allergenin tartary buckwheat. Experiments were carried out to explore the interaction between TBt and Cu2+ by fluorescencespectroscopy, analyze the structural change of TBt by circular dichroism (CD) spectroscopy and native polyacrylamide gelelectrophoresis (PAGE), and identify the effect of Cu2+ on its IgG binding capacity by indirect ELISA and inhibitory ELISA.The results of the fluorescence spectroscopic analysis indicated that Cu2+ could be bound to TBt at a molar ratio of 1:1. CDanalysis showed the secondary structure of TBt did not change, but the spatial structure of TBt was changed in native PAGE.Briefly, the spatial structures of TBt changed into hexamers after interaction with Cu2+. Inhibitory ELISA and indirect ELISAshowed that TBt became a hexamer, and a part of epitopes were covered and the IgG binding capacity was decreased.

Key words: tartary buckwheat, allergenic protein, metallic ions, allergenicity