From Molecule to Tissue: XIII European Conference on the Spectroscopy of Biological Molecules, Palermo, Italy, August 28–September 2, 2009, Part 2 of 2View this Special Issue
A. Goldsztein, S. Babar, M. Voué, J. De Coninck, J. Conti, J. Marchand-Brynaert, S. Devouge, F. Homblé, E. Goormaghtigh, "Gastric ATPase phosphorylation/dephosphorylation monitored by new FTIR-based BIA–ATR biosensors", Journal of Spectroscopy, vol. 24, Article ID 793594, 4 pages, 2010. https://doi.org/10.3233/SPE-2010-0402
Gastric ATPase phosphorylation/dephosphorylation monitored by new FTIR-based BIA–ATR biosensors
Biosensors are composite devices suitable for the investigation of receptor–ligand interactions. In this paper we present the specific application to a membrane embedded protein of a new sensor device, so-called BIA–ATR, based on Attenuated Total Reflection–Fourier Transform Infrared (ATR–FTIR) spectroscopy. It consists in a functionalised ATR germanium crystal whose surface has been covalently modified to adsorb a biomembrane. Detection of the ligand–receptor interaction is achieved using FTIR spectroscopy. We report the specific detection of the phosphorylation/dephosphorylation of the H+/K+ gastric ATPase. The H+, K+-ATPase is a particularly large protein entity. This glycosylated protein contains more than 1300 residues and is embedded in a lipid membrane. Yet we demonstrate that the BIA–ATR sensor is capable of monitoring the binding of a single phosphate on such a large protein entity. Furthermore, we also demonstrate the potential of the approach to monitor the kinetics of binding and dissociation of the ligand.
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