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Updated: May 16, 2026
Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms
Published on: April 17, 2017
Recombinant antibody fragments allow repeated measurements of C-reactive protein with a quartz crystal microbalance
Laila Al-Halabi1, Anne Balck, Monika Michalzik
1Institute of Biochemistry, Biotechnology and Bioinformatics, Department of Biotechnology, Technische Universität Braunschweig, Braunschweig, Germany.
Abstract:
C-reactive protein (CRP) is a serum marker highly upregulated in inflammation after bacterial infection. Robust, reliable and quick quantification of CRP would be a substitute for erythrocyte sedimentation rate (ESR) with superior diagnostic value. Quartz crystal microbalance (QCM) based sensors coated with specific antibodies and integrated into lab-on-chip systems are in development for rapid point of care quantification. In this study, we isolated three CRP specific single chain (sc)Fv antibody fragments using phage display from an antibody gene library. Their affinities ranged from 2.7 × 10(-8) to 1.0 × 10(-8) M when measured by surface plasmon resonance. ScFv antibody fragment LA13-IIE3 showed best affinity, high long-term stability and remarkable resistance to denaturation. This scFv antibody fragment was coupled to a QCM sensor. CRP quantification in up to 15 samples sequentially measured on the same sensor with intermitting regeneration by buffer was demonstrated.
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