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Measurement of protein binding with vastly improved time resolution using a quartz crystal microbalance driven at a fixed frequency
Wolfson School of Mechanical, Electrical and Manufacturing Engineering, Epinal Way, Loughborough, Loughborough University, LE11 3TU, UK.
KTH, School of Engineering Sciences (SCI), Applied Physics, Biophysics. (Önfelt Lab)ORCID iD: 0000-0001-6443-878X
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW , UK.
KTH, School of Electrical Engineering and Computer Science (EECS), Micro and Nanosystems.ORCID iD: 0000-0001-8248-6670
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2017 (English)Conference paper, Poster (with or without abstract) (Other academic)
Abstract [en]

Introduction: Quartz crystal microbalance (QCM) is commonly used to study biomolecular binding by measuring shifts in resonance frequency of a quartz-crystal-oscillator. However, the currently used methods like impedance analysis or QCM-D, which require repeated sweeps or ringing, are limited in time resolution (~1 second) due to the need for averaging. This restricts our ability to study transient biomolecular processes, which occur in sub-millisecond time scale. A novel technique has been reported here that allows quantification of resonance frequency of a quartz-crystal-oscillator with significantly improved time resolution by driving and measuring continuously at a constant frequency within the resonance bandwidth. 

Method: The reactive component of the experimentally obtained impedance is utilized for the estimation of resonance frequency from the Butterworth Van-dyke (BVD) model of a quartz-crystal-oscillator, assuming that changes in motional inductance and capacitance around resonance are negligible. Triplicate sets of experiments involving the binding of streptavidin with a biotin functionalized 14.3 MHz quartz oscillator surface were performed. Intermittent frequency sweeps and fixed frequency drives, both of 0.1 second duration and around 14.3 MHz, were taken at intervals of 2 minutes under the flow of phosphate-buffer-saline (PBS buffer) before and after injection of streptavidin. 

Results: The average shift in resonance frequency from the baseline (measurements before streptavidin injection) due to streptavidin-biotin binding, calculated from the fixed frequency drive or FFD (148 Hz) was within 1% of that estimated from the frequency sweep method by fitting the experimentally recorded impedance employing the BVD model (149 Hz). 

Discussion: The agreement of the FFD with conventional frequency sweep method suggests that protein binding can be quantified with reasonable accuracy from each impedance data point, which with our set-up is recorded at 30 kHz sampling rate. This gives a time resolution of 0.03 millisecond, which is about 4 orders of magnitude improvement over the state-of-the-art.

Place, publisher, year, edition, pages
2017.
National Category
Medical Engineering
Research subject
Biotechnology
Identifiers
URN: urn:nbn:se:kth:diva-249535OAI: oai:DiVA.org:kth-249535DiVA, id: diva2:1304625
Conference
5th International conference on Bio-Sensing Technology, 7 - 10 May 2017, Riva Del Garda, Italy
Note

QC 20190522

Available from: 2019-04-12 Created: 2019-04-12 Last updated: 2019-05-22Bibliographically approved

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Sandström, Niklasvan der Wijngaart, Wouter

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