Affinity Interactions between Phenylboronic Acid‐Carrying Self‐Assembled Monolayers and Flavin Adenine Dinucleotide or Horseradish Peroxidase

摘要: A method is provided for the recognition of glycated molecules based on their binding affinities to boronate-carrying monolayers. The affinity interaction flavin adenine dinucleotide (FAD) and horseradish peroxidase (HRP) with phenylboronic acid monolayers gold was investigated by using voltammetric microgravimetric methods. Conjugates 3-aminophenylboronic 3,3'-dithiodipropionic di(N-hydroxysuccinimide ester) or 11-mercaptoundecanoic were prepared self-assembled surfaces generate FAD bound this modified surface recognized a pair redox peaks formal potential -0.433 V in 0.1 M phosphate buffer solution, pH 6.5. Upon addition sugar buffer, could be replaced, indicating that reversible. Voltammetric, mass measurements, photometric activity assays show HRP can also interface. This reversible, replaced sorbitol removed acidic solution. effects pH, incubation time, concentration H(2)O(2) studied comparing catalytic reduction presence electron-donor thionine. current HRP-loaded electrode proportional concentrations solution range between 5 microg mL(-1) mg linear slope 3.34 microA mL mg(-1) correlation coefficient 0.9945.