Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
744435 | Sensors and Actuators B: Chemical | 2011 | 7 Pages |
The surface plasmon resonance (SPR) biosensors have been used to detect various target analytes by using highly specific antigen–antibody interactions. In this work, a parylene film modified to have primary amine groups was applied as a linker layer of the SPR biosensor, and the primary amine groups were used for the covalent immobilization of proteins to the SPR biosensor. The feasibility of the parylene film as a linker layer was presented by estimating the influence of the parylene film on the SPR measurement parameters, such as the sensitivity and the detection range. Then, a model protein called horseradish peroxidase (HRP) was used to demonstrate the improved immobilization efficiency as well as the sensitivity of the SPR biosensor with the parylene-A film. Additionally, a reconstruction method of the immunoaffinity layer was presented by using oxygen plasma.