No abstract

A monomolecular layer of glucose oxidase (GOD) was immobilized on an SnO2 electrode via glutaraldehyde-bridged covalent bonding of GOD to the amino moieties of an octadecylamine Langmuir–Blodgett film. The performance of the electrode as an amperometric glucose sensor was investigated.

A novel antibody-polymer conjugation method termed open-sandwich molecular imprinting (OS-MIP) has been proposed to produce a specific recognition matrix in the presence of a target antigen. The resultant carboxymethyldextran matrix conjugated with two separate antibody variable region fragments imprinted with the cognate antigen showed higher antigen-binding capacity than non-imprinted ones and was successfully used to sensitively monitor multiple antigen binding/desorption events by a surface plasmon resonance biosensor. Furthermore, when each fragment was labeled with different fluorophores before conjugation, the fluorescence signals of the matrix made by OS-MIP clearly showed an antigen concentration dependent increase in Förster resonance energy transfer between the two dyes. By using a combination of various methods for detecting interaction, OS-MIP will be a useful platform for detecting various targets from small molecules to proteins with high sensitivity and specificity.

Glucose oxidase was chemically immobilized on an SnO2 electrode via 1) 2,4,6-trichloro-1,3,5-triazine, 2) 3-aminopropyltriethoxysilane and glutaraldehyde, or 3) crosslinkage of enzyme molecules by glutaraldehyde. These enzyme-immobilized electrodes were compared regarding the performance as amperometric glucose sensors.