Microfluidics Devices Integrating Microcavity Surface-Plasmon-Resonance Biosensors: Glucose Oxidase Enzymatic Activity

Dragos Amarie; Abdelkrim Alileche; Bogdan Dragnea; James A. Glazier

Microfluidics Devices Integrating Microcavity Surface-Plasmon-Resonance Biosensors: Glucose Oxidase Enzymatic Activity

Dragos Amarie, Abdelkrim Alileche, Bogdan Dragnea, James A. Glazier

Biochemistry, Chemistry & Physics

Indiana University Bloomington

Research output: Contribution to conference › Presentation

Abstract

We describe the integration of 1-µm-diameter microcavity surface-plasmon-resonance sensors with microfluidics, test their sensitivity to refractive-index changes, relate their response to the response units (RU) used in Biacore instruments and demonstrate their biosensing capability by distinguishing the interaction of glucose oxidase (160kDa) with its natural substrate (βD-Glucose, 180Da) from its interactions with non-specific substrates (L-Glucose, D-Mannose or 2-DeoxyD-Glucose). The same protocol run on a Biocore-3000 reveals no internation between glucose oxidase and the substrates. The biosensor can detect binding of about 25,000 proteins (6.5 fg), 10⁶ times fewer than classical surface-plasmon-resonance biosensors.

Original language	American English
State	Published - Aug 2009
Event	q-Bio Conference on Cellular Information Processing - Santa Fe, NM Duration: Aug 1 2009 → …

Conference

Conference	q-Bio Conference on Cellular Information Processing
Period	08/1/09 → …

Disciplines

Biology

Keywords

Glucose oxidase enzymatic activity
Integrating microcavity surface-plasmon-resonance biosensors
Microfluidics devices

Cite this

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title = "Microfluidics Devices Integrating Microcavity Surface-Plasmon-Resonance Biosensors: Glucose Oxidase Enzymatic Activity",

abstract = " We describe the integration of 1-µm-diameter microcavity surface-plasmon-resonance sensors with microfluidics, test their sensitivity to refractive-index changes, relate their response to the response units (RU) used in Biacore instruments and demonstrate their biosensing capability by distinguishing the interaction of glucose oxidase (160kDa) with its natural substrate (βD-Glucose, 180Da) from its interactions with non-specific substrates (L-Glucose, D-Mannose or 2-DeoxyD-Glucose). The same protocol run on a Biocore-3000 reveals no internation between glucose oxidase and the substrates. The biosensor can detect binding of about 25,000 proteins (6.5 fg), 10⁶ times fewer than classical surface-plasmon-resonance biosensors.",

keywords = "Glucose oxidase enzymatic activity, Integrating microcavity surface-plasmon-resonance biosensors, Microfluidics devices",

author = "Dragos Amarie and Abdelkrim Alileche and Bogdan Dragnea and Glazier, {James A.}",

year = "2009",

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language = "American English",

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TY - CONF

T1 - Microfluidics Devices Integrating Microcavity Surface-Plasmon-Resonance Biosensors: Glucose Oxidase Enzymatic Activity

AU - Amarie, Dragos

AU - Alileche, Abdelkrim

AU - Dragnea, Bogdan

AU - Glazier, James A.

PY - 2009/8

Y1 - 2009/8

N2 - We describe the integration of 1-µm-diameter microcavity surface-plasmon-resonance sensors with microfluidics, test their sensitivity to refractive-index changes, relate their response to the response units (RU) used in Biacore instruments and demonstrate their biosensing capability by distinguishing the interaction of glucose oxidase (160kDa) with its natural substrate (βD-Glucose, 180Da) from its interactions with non-specific substrates (L-Glucose, D-Mannose or 2-DeoxyD-Glucose). The same protocol run on a Biocore-3000 reveals no internation between glucose oxidase and the substrates. The biosensor can detect binding of about 25,000 proteins (6.5 fg), 10⁶ times fewer than classical surface-plasmon-resonance biosensors.

AB - We describe the integration of 1-µm-diameter microcavity surface-plasmon-resonance sensors with microfluidics, test their sensitivity to refractive-index changes, relate their response to the response units (RU) used in Biacore instruments and demonstrate their biosensing capability by distinguishing the interaction of glucose oxidase (160kDa) with its natural substrate (βD-Glucose, 180Da) from its interactions with non-specific substrates (L-Glucose, D-Mannose or 2-DeoxyD-Glucose). The same protocol run on a Biocore-3000 reveals no internation between glucose oxidase and the substrates. The biosensor can detect binding of about 25,000 proteins (6.5 fg), 10⁶ times fewer than classical surface-plasmon-resonance biosensors.

KW - Glucose oxidase enzymatic activity

KW - Integrating microcavity surface-plasmon-resonance biosensors

KW - Microfluidics devices

UR - http://cnls.lanl.gov/q-bio/wiki/images/9/91/076_Amarie.pdf

M3 - Presentation

T2 - q-Bio Conference on Cellular Information Processing

Y2 - 1 August 2009

ER -

Microfluidics Devices Integrating Microcavity Surface-Plasmon-Resonance Biosensors: Glucose Oxidase Enzymatic Activity

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