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Because of the medical interest in the neuroscience, GluR1 is one of the important subunits of the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPAR). AMPARs are ionotoropic glutamate receptors, which are mediating fast synaptic transmission and are crucial for plasticity in the brain. On the other hand, KYNA has been suggested to have neuroprotective activity and it has been considered for apply in therapy in certain neurobiological disorders. In this article the adsorption of the GluR1(201-230) and GluR1(231-259) peptides were studied on gold biosensor chip. The peptides were chemically bonded onto the gold surface via thiol group of L-cysteine resulted in the formation of peptide monolayer on the SPR chip surface. Because the GluR1(231-259) peptide does not contain L-cysteine the Val256 was replaced by Cys256. The cross sectional area and the surface orientation of the studied peptides were determined by SPR and theoretical calculations (LOMETS) as well. The binding capability of KYNA on the peptide monolayer was studied in the concentration range of 0.1-5.0 mM using 150 mM NaCl ionic strength at pH 7.4 (+/- 0.02) in phosphate buffer solutions. In order to determine the binding enthalpy the experiments were carried out between +10 degrees C and +40 degrees C. The heat of adsorption was calculated by using adsorption isotherms at different surface loading of KYNA on the SPR chip. (C) 2014 Elsevier B.V. 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