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Abstract: In order to understand the chemical mechanism and optimal conditions of the molecular imprinting, the interaction between 3-aminophenylboronic acid (APBA) and bovine serum albumin (BSA) was investigated using fluorescence quenching method with many factors, as the pH value, ionic strength and others, which maybe influence the interaction. The research results indicate that under appropriate ionic strength and pH 6.25, the fluorescence quenching shows that APBA strongly bound with the tryptophan of BSA, and the complex was formed with a molar ratio of 2 : 1. Their apparent binding constant is K-A = 1.0 x 10(11) L-2.mol(-2), so their chemical bindings between donor BSA and acceptor APBA are relatively strong. According to the results, the interaction mechanism between APBA and BSA is predicted. During following research, it will be entirely possible to separate or enrich BSA composition, maybe it could improve imprinting and eluting efficiency greatly
Template and target information: protein, bovine serum albumin, BSA
Author keywords: 3-aminophenylboronic acid, Bovine serum albumin, fluorescence quenching, molecularly imprinting