Recombinant antibody fragments allow repeated measurements of C-reactive protein with a quartz crystal microbalance immunosensor

Al-Halabi, Laila; Balck, Anne; Michalzik, Monika; Fröde, David; Büttgenbach, S.; Hust, Michael; Schirrmann, Thomas; Dübel, Stefan

doi:10.4161/mabs.22374

Cited by 10 publications

(8 citation statements)

References 25 publications

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“…10). For the detection of CRP (Bio-Rad, Native Human C-Reactive Protein 1707-2029), recombinant antibodies (scFv-Fc) generated in vitro by antibody phage-display, with binding properties specially engineered to fit to the measurement principle (Al-Halabi et al, 2013) have to be bound to the SAM. This step defines which substances will be measured with the QCM, as such recombinant antibodies made by in vitro evolution can be obtained to specifically detect almost any protein and even many non-proteinous biomolecules (Frenzel et al, 2012;Dübel et al, 2010).…”

Section: Measurements and Resultsmentioning

confidence: 99%

Low-cost, in-liquid measuring system using a novel compact oscillation circuit and quartz-crystal microbalances (QCMs) as a versatile biosensor platform

Beißner

Thies

Bechthold

et al. 2017

J. Sens. Sens. Syst.

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Abstract. Quartz-crystal microbalances (QCMs) are commercially available mass sensors which mainly consist of a quartz resonator that oscillates at a characteristic frequency, which shifts when mass changes due to surface binding of molecules. In addition to mass changes, the viscosity of gases or liquids in contact with the sensor also shifts the resonance but also influences the quality factor (Q-factor). Typical biosensor applications demand operation in liquid environments leading to viscous damping strongly lowering Q-factors. For obtaining reliable measurements in liquid environments, excellent resonator control and signal processing are essential but standard resonator circuits like the Pierce and Colpitts oscillator fail to establish stable resonances. Here we present a lowcost, compact and robust oscillator circuit comprising of state-of-the-art commercially available surface-mount technology components which stimulates the QCMs oscillation, while it also establishes a control loop regulating the applied voltage. Thereby an increased energy dissipation by strong viscous damping in liquid solutions can be compensated and oscillations are stabilized. The presented circuit is suitable to be used in compact biosensor systems using custom-made miniaturized QCMs in microfluidic environments. As a proof of concept we used this circuit in combination with a customized microfabricated QCM in a microfluidic environment to measure the concentration of C-reactive protein (CRP) in buffer (PBS) down to concentrations as low as 5 µg mL −1 .

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Section: Measurements and Resultsmentioning

confidence: 99%

Low-cost, in-liquid measuring system using a novel compact oscillation circuit and quartz-crystal microbalances (QCMs) as a versatile biosensor platform

Beißner

Thies

Bechthold

et al. 2017

J. Sens. Sens. Syst.

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“…The method has been frequently used as a means of detection of specific disease related protein markers in serum. 68 In addition to simple molecular binders the sensor surface can be decorated by complex structures like supported model lipid membranes or cell derived membranes enabling studies of membrane binders like pore-forming proteins and others. 62 …”

Section: Quartz Crystal Microbalancementioning

confidence: 99%

How to Study Protein-protein Interactions

Podobnik¹,

Kraševec²,

Zavec³

et al. 2016

ACSi

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In memory of prof. dr. Janko Jamnik. AbstractPhysical and functional interactions between molecules in living systems are central to all biological processes. Identification of protein complexes therefore is becoming increasingly important to gain a molecular understanding of cells and organisms. Several powerful methodologies and techniques have been developed to study molecular interactions and thus help elucidate their nature and role in biology as well as potential ways how to interfere with them. All different techniques used in these studies have their strengths and weaknesses and since they are mostly employed in in vitro conditions, a single approach can hardly accurately reproduce interactions that happen under physiological conditions. However, complementary usage of as many as possible available techniques can lead to relatively realistic picture of the biological process. Here we describe several proteomic, biophysical and structural tools that help us understand the nature and mechanism of these interactions.

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“…For this purpose, we used an antibody sandwich consisting of two recombinant CRP-specific antibodies (scFv-Fc) which were isolated from a human antibody library by phage display and engineered for the use on a microchip [7,8]. The first antibody is immobilized on the surface of the QCM sensor while the second antibody is added after the target analyte is captured on the QCM with the aim to increase the total bound mass.…”

Section: Introductionmentioning

confidence: 99%

Microfluidic quartz-crystal-microbalance (QCM) sensors with specialized immunoassays for extended measurement range and improved reusability

Thies¹,

Kühn

Thrmann³

et al. 2017

Microelectronic Engineering

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Recombinant antibody fragments allow repeated measurements of C-reactive protein with a quartz crystal microbalance immunosensor

Abstract: (2013) Recombinant antibody fragments allow repeated measurements of C-reactive protein with a quartz crystal microbalance immunosensor, mAbs, 5:1, 140-149,

Cited by 10 publications

References 25 publications

Low-cost, in-liquid measuring system using a novel compact oscillation circuit and quartz-crystal microbalances (QCMs) as a versatile biosensor platform

Low-cost, in-liquid measuring system using a novel compact oscillation circuit and quartz-crystal microbalances (QCMs) as a versatile biosensor platform

How to Study Protein-protein Interactions

Microfluidic quartz-crystal-microbalance (QCM) sensors with specialized immunoassays for extended measurement range and improved reusability

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