Parallel microfluidic surface plasmon resonance imaging arrays

Ouellet, Éric; Lausted, Christopher; Lin, Tengfei; Yang, Cheng Wei Tony; Hood, Leroy; Lagally, Eric T.

doi:10.1039/b920589f

Cited by 119 publications

(95 citation statements)

References 41 publications

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“…SPR-based measurements have been integrated with microfluidic devices (19,20) to achieve higher degrees of parallelization (21). Yet proof of concept demonstrations have made use of only a small fraction of the proposed throughput and often restrict their measurements to protein-antibody interactions with high affinities and long half-lives (21)(22)(23). On the other hand, low affinity or transient interactions, which are more relevant to biological systems, have not been measured in a high-throughput format.…”

mentioning

confidence: 99%

“…Current methods used for kinetic rate measurements are generally based on surface plasmon resonance (SPR) (18) such as BioRad's ProteOn XPR36 6 × 6 array system, which measures 36 interactions in a single run. SPR-based measurements have been integrated with microfluidic devices (19,20) to achieve higher degrees of parallelization (21). Yet proof of concept demonstrations have made use of only a small fraction of the proposed throughput and often restrict their measurements to protein-antibody interactions with high affinities and long half-lives (21)(22)(23).…”

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confidence: 99%

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Massively parallel measurements of molecular interaction kinetics on a microfluidic platform

Geertz

Shore

Maerkl

2012

Proc. Natl. Acad. Sci. U.S.A.

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Quantitative biology requires quantitative data. No high-throughput technologies exist capable of obtaining several hundred independent kinetic binding measurements in a single experiment. We present an integrated microfluidic device (k-MITOMI) for the simultaneous kinetic characterization of 768 biomolecular interactions. We applied k-MITOMI to the kinetic analysis of transcription factor (TF)-DNA interactions, measuring the detailed kinetic landscapes of the mouse TF Zif268, and the yeast TFs Tye7p, Yox1p, and Tbf1p. We demonstrated the integrated nature of k-MITOMI by expressing, purifying, and characterizing 27 additional yeast transcription factors in parallel on a single device. Overall, we obtained 2,388 association and dissociation curves of 223 unique molecular interactions with equilibrium dissociation constants ranging from 2 × 10 −6 M to 2 × 10 −9 M, and dissociation rate constants of approximately 6 s −1 to 8.5 × 10 −3 s −1 . Association rate constants were uniform across 3 TF families, ranging from 3.7 × 10 6 M −1 s −1 to 9.6 × 10 7 M −1 s −1 , and are well below the diffusion limit. We expect that k-MITOMI will contribute to our quantitative understanding of biological systems and accelerate the development and characterization of engineered systems.biochemistry | biophysics | systems biology S ystems and synthetic biology, as well as the computational models and engineering-based approaches they employ, rely heavily on quantitative data (1, 2). Thus far, efforts in systems biology have mainly focused on cataloging and mapping genomes and proteomes. Genome sequencing and gene expression analysis have provided insight into genome architecture (3-6), and functional genomics approaches, including high-throughput protein-based methods (7-15), mapped network topologies.Although the number of known protein-protein and protein-DNA interactions is already substantial, the information describing such networks is predominantly qualitative and binary in nature. It is also becoming clear that network topologies alone are not sufficient to model complex biological processes. Precise quantitative information describing every interaction in a network would be tremendously valuable (2), yet binding affinities are known for only a small fraction of interactions (16, 17) and kinetic information hardly exists at all. This dearth of quantitative interaction data is due to a lack of high-throughput technologies capable of measuring kinetic rates of biomolecular interactions. Current methods used for kinetic rate measurements are generally based on surface plasmon resonance (SPR) (18) such as BioRad's ProteOn XPR36 6 × 6 array system, which measures 36 interactions in a single run. SPR-based measurements have been integrated with microfluidic devices (19, 20) to achieve higher degrees of parallelization (21). Yet proof of concept demonstrations have made use of only a small fraction of the proposed throughput and often restrict their measurements to protein-antibody interactions with high affinities and long half-lives...

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mentioning

confidence: 99%

mentioning

confidence: 99%

Massively parallel measurements of molecular interaction kinetics on a microfluidic platform

Geertz

Shore

Maerkl

2012

Proc. Natl. Acad. Sci. U.S.A.

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“…Traditional inorganic microfluidic device substrates are glass and silicon, which originated from the semiconductor industry and benefit from mature microfabrication techniques. For specialized detection methods such as surface plasmon resonance (SPR), 8,9,49 Raman spectroscopy, 69 and electrochemical analysis, 35,36,70 protein is immobilized on metal films deposited on a glass or silicon surface. Silicon and glass share a similar surface chemistry, thus the route to immobilization is similar.…”

Section: Immobilization Surfacementioning

confidence: 99%

“…[38][39][40][41][42] Laboratory-grade assays such as polyacrylamide gel electrophoresis (PAGE) based immunoassays, [43][44][45] isoelectric focusing (IEF), 21 and Western blotting [18][19][20]22,24,46 provide qualitative and/or quantitative information on multiple proteins, even in complex biological fluids. Questions spanning from protein-protein interactions, 47,48 and protein binding kinetics, 49,50 to post-translational modifications 23,51 have all been pursued using analytical technologies in microfluidic formats. Recent reviews by Hanares et al, 9 Bange et al, 10 and Ng et al 8 are recommended as excellent overviews of immunoassay advances.…”

Section: Introductionmentioning

confidence: 99%

Protein immobilization techniques for microfluidic assays

2013

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Microfluidic systems have shown unequivocal performance improvements over conventional bench-top assays across a range of performance metrics. For example, specific advances have been made in reagent consumption, throughput, integration of multiple assay steps, assay automation, and multiplexing capability. For heterogeneous systems, controlled immobilization of reactants is essential for reliable, sensitive detection of analytes. In most cases, protein immobilization densities are maximized, while native activity and conformation are maintained. Immobilization methods and chemistries vary significantly depending on immobilization surface, protein properties, and specific assay goals. In this review, we present trade-offs considerations for common immobilization surface materials. We overview immobilization methods and chemistries, and discuss studies exemplar of key approaches—here with a specific emphasis on immunoassays and enzymatic reactors. Recent “smart immobilization” methods including the use of light, electrochemical, thermal, and chemical stimuli to attach and detach proteins on demand with precise spatial control are highlighted. Spatially encoded protein immobilization using DNA hybridization for multiplexed assays and reversible protein immobilization surfaces for repeatable assay are introduced as immobilization methods. We also describe multifunctional surface coatings that can perform tasks that were, until recently, relegated to multiple functional coatings. We consider the microfluidics literature from 1997 to present and close with a perspective on future approaches to protein immobilization.

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“…Due to the dependence of the resonance condition on the refractive index of the material contacting the metal, surface plasmon resonance (SPR) based techniques have been widely applied into biological and chemical detection [1,2]. Integrated with microfluidic, high-throughput SPR sensors have been realized for various applications [3,4].…”

Section: Introductionmentioning

confidence: 99%

Surface Plasmon Resonance Phase-Sensitive Imaging (Spr-Pi) Sensor Based on a Novel Prism Phase Modulator

Ye¹,

Yang²,

Jiang³

et al. 2014

PIER

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Abstract-A novel prism phase modulator (PPM) for phase difference modulation between p-and s-polarization lights in a surface plasmon resonance phase-sensitive imaging sensor is proposed in this paper. The PPM consists of a rhombic prism (to obtain a curve of phase difference between the two polarizations), a rotation stage and a mirror. The PPM shows great modulation stability and helps to achieve a high detection resolution. Surface plasmon resonance phase imaging is realized with a microfluidic device and a CCD camera. Experimental result shows that the detection resolution of our SPR-PI sensor based on phase-interrogation method is 7.61 × 10 −7 RIU with hydrous samples, which is 16 times improved compared with that based on intensity-interrogation. Real-time monitoring of the interaction between Angiogenin and anti-Angiogenin is also illustrated.

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Parallel microfluidic surface plasmon resonance imaging arrays

Cited by 119 publications

References 41 publications

Massively parallel measurements of molecular interaction kinetics on a microfluidic platform

Massively parallel measurements of molecular interaction kinetics on a microfluidic platform

Protein immobilization techniques for microfluidic assays

Surface Plasmon Resonance Phase-Sensitive Imaging (Spr-Pi) Sensor Based on a Novel Prism Phase Modulator

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