Surface plasmon resonance sensor based on an array of diffraction gratings for highly parallelized observation of biomolecular interactions

• Published in: Sensors and actuators. B, Chemical Vol. 129; no. 1; pp. 303 - 310
• Main Authors: Dostálek, Jakub, Homola, Jiří
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 29.01.2008
• Subjects: Arrays; Biomolecular interaction analysis; Biosensors; Channels; Chips; Detection; Diffraction grating; Diffraction gratings; Environmental monitoring; High-throughput screening; Immunoassay; Plasmons; Sensors; Surface plasmon resonance; Surface plasmons; Two dimensional; Diffraction grating; Immunoassay; High-throughput screening; Surface plasmon resonance; Biosensors; Environmental monitoring; Surface plasmons; Biomolecular interaction analysis
• ISSN: 0925-4005; 1873-3077
• DOI: 10.1016/j.snb.2007.08.012

We report a novel surface plasmon resonance (SPR) sensor for highly parallelized biomolecular interaction analysis (BIA). This sensor utilizes an array detection format and angular spectroscopy of surface plasmons on a two-dimensional array of metallic diffraction gratings. Each diffraction grating on a sensor chip serves both as an SPR coupler and a sensing channel in which refractive index changes induced by biomolecular interaction events are measured. We theoretically optimized the diffraction grating-based sensor to yield maximum resolution in the measurement of refractive index changes. Based on this study, we developed a prototype sensor instrument which enables parallel measurements with high-refractive index resolution (5 × 10 −7 RIU) in large number of sensing channels (120). The instrument consists of a two-dimensional array of sensing channels on a sensor chip, a fluidic system for sample delivery, and an SPR optical readout system. By using this instrument and micro spotting to produce a chip array, we evaluated the cross-binding of antibodies against a selected set of endocrine-disrupting compounds (atrazine, 2,4-dichlorophenoxyaceic acid, 4-nonylphenol and benzo[ a]pyrene) to respective protein–analyte conjugates.