Surface plasmon resonance protein sensor using Vroman effect

Choi, Seokheun; Yang, Yongmo; Chae, Junseok

doi:10.1016/j.bios.2008.07.036

Cited by 56 publications

(34 citation statements)

References 17 publications

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“…The phenomena and characterization of protein adsorption at the solid/solution interface are essential for developing biocompatible materials, various biotechnological processes, and diagnostic techniques [25]. In particular, the adsorption of blood proteins on medical devices and their subsequent displacement result in false errors in diagnostics [26].…”

Section: Biosensingmentioning

confidence: 99%

A High-Quality-Factor Film Bulk Acoustic Resonator in Liquid for Biosensing Applications

Zhang

Choi

et al. 2011

J. Microelectromech. Syst.

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We report a high-quality-factor (Q) film bulk acoustic resonator (FBAR) operating in liquid environments. By integrating a microfluidic channel to a longitudinal-mode FBAR, a Q of up to 150 is achieved with direct liquid contacting. A transmission line model is used to theoretically predict the Q behavior of the FBAR. The model suggests an oscillatory pattern of Q as a function of the channel thickness and the acoustic wavelength in the liquid, which is experimentally verified by precisely controlling the channel thickness. This FBAR biosensor is characterized in liquids for the real-time in situ monitoring of the competitive adsorption/exchange of proteins, the Vroman effect. The FBAR offers a minimum detectable mass of 1.35 ng/cm 2 and is successfully implemented in a Pierce oscillator as a portable sensing module.[2010-0220]

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Section: Biosensingmentioning

confidence: 99%

A High-Quality-Factor Film Bulk Acoustic Resonator in Liquid for Biosensing Applications

Zhang

Choi

et al. 2011

J. Microelectromech. Syst.

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“…The ability of the former to detect various protein interactions has been already demonstrated [17][18][19]. In contrast to SPR sensors, BSW sensors are metal free.…”

Section: Introductionmentioning

confidence: 99%

Detection of protein aggregation with a Bloch surface wave based sensor

Paeder

Musi

Hvozdara

et al. 2011

Sensors and Actuators B: Chemical

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“…The adsorption of any protein onto a solid surface is a strong function of hydrophobic attraction. Hydrophilic residues form the orientation of the adsorbed protein and do not take part in the adsorption process itself (Latour 2005;Choi et al 2008). Therefore, proteins rapidly adsorb onto a hydrophobic surface, unfold and spread their hydrophobic core over the surface.…”

Section: Real Time Monitoring Of Sam Desorptionmentioning

confidence: 99%

A regenerative biosensing surface in microfluidics using electrochemical desorption of short-chain self-assembled monolayer

Choi

Chae

2009

Microfluid Nanofluid

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We report a novel method to regenerate a biosensor surface in microfluidics. By applying a low DC voltage (0.9 V) between two electrodes submerged in phosphate buffered saline, the sensing surface resets to be reusable and reconfigurable; streptavidin-bound COOH-SAM completely desorbs and CH 3 -terminated self-assembled monolayer (SAM) forms on the sensing surface to capture the subsequent target molecule, fibrinogen, in a microfluidic device. The biomolecular interactions are monitored by surface plasmon resonance in real time, and ellipsometry and linear sweep voltammetry are used to evaluate the results. Despite much study on the theoretical mechanism of electrochemical SAM desorption, relatively little research has been carried out on its full integration into a microfluidic system. This is because of electrode peeling-off and electrolysis occurring at a similar potential to the potential of the SAM desorption. In this paper, we report that the potential for the reductive desorption of thiol SAMs depends on the length of the alkyl chin, the type of terminal groups and the binding of proteins and that our approach using short-chain SAMs (n \ 3) can be a good candidate to minimize these limitations. While the surface modified by proteins on the long-chain SAMs (n [ 10) needs more than 1.0 V between two electrodes to be completely regenerated, the protein-bound surface on the short-chain SAMs (n \ 3) does around 0.9-DC voltage. Linear sweep voltammetry demonstrates that hydrogen evolution (approx. -1.2 V) does not overlap the shortchain SAM desorption and the electrode does not peel off during the desorption process as well. It is shown that the modified proteins in the same microfluidic device are still stable even after 10 cycles showing a relative standard deviation lower than 1.86%.

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Surface plasmon resonance protein sensor using Vroman effect

Cited by 56 publications

References 17 publications

A High-Quality-Factor Film Bulk Acoustic Resonator in Liquid for Biosensing Applications

A High-Quality-Factor Film Bulk Acoustic Resonator in Liquid for Biosensing Applications

Detection of protein aggregation with a Bloch surface wave based sensor

A regenerative biosensing surface in microfluidics using electrochemical desorption of short-chain self-assembled monolayer

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