水晶振動子型バイオセンサーによる生体分子間相互作用の研究

概要

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Two serine protease inhibitors from soybeans, Kunitz type soybean trypsin inhibitor (STI) and Bowman-Birk inhibitor (BBI) were immobilized via an alkanethiol onto a gold surface on a highly sensitive 21 MHz AT-cut quartz-crystal microbalance (QCM) chip. The QCM exhibited a significant decrease in frequency responding to serine protease addition. The dissociation constants (Kd) for the interactions of STI-bovine pancreatic trypsin, BBI-bovine pancreatic trypsin, and BBI-bovine pancreatic chymotrypsin were determined, respectively, to be 47.0 nM, 83.6 nM, and 52.9 nM. The data suggest that the inhibitors were immobilized on the gold surface of QCM in a possible orientation to react with corresponding serine proteases. Based on the observations, it may be concluded that combining protease inhibitor and protease recognition events with an appropriate QCM transducer can yield sensor devices highly suitable for detection of proteases in food, clinical and biodefense areas.