TY  - JOUR
AU  - Csapó, Edit
AU  - Bogár, Ferenc
AU  - Juhász, Ádám
AU  - Sebők, Dániel
AU  - Szolomájer, János
AU  - Tóth, Gábor
AU  - Majláth, Zsófia
AU  - Vécsei, László
AU  - Dékány, Imre
TI  - Determination of binding capacity and adsorption enthalpy between Human Glutamate Receptor (GluR1) peptide fragments and kynurenic acid by surface plasmon resonance experiments. Part 2: Interaction of GluR1270–300 with KYNA
JF  - COLLOIDS AND SURFACES B: BIOINTERFACES
J2  - COLLOID SURFACE B
VL  - 133
PY  - 2015
SP  - 66
EP  - 72
PG  - 7
SN  - 0927-7765
DO  - 10.1016/j.colsurfb.2015.04.044
UR  - https://m2.mtmt.hu/api/publication/2908470
ID  - 2908470
N1  - Funding Agency and Grant Number: European Union; State of Hungary; European Social Fund [TAMOP-4.2.2.A-11/1/KONV-2012-0047]; Hungarian Brain Research Program (NAP) [KTIA-13-NAP-AIII/9]; EUROHEADPAIN [602633]\n Funding text: This research was supported by the European Union and the State of Hungary, co-financed by the European Social Fund in the framework of TAMOP-4.2.2.A-11/1/KONV-2012-0047, by the Hungarian Brain Research Program (NAP. Grant No. KTIA-13-NAP-AIII/9) and by EUROHEADPAIN (FP7-Health 2013-Innovation; Grant No. 602633). The authors thank Judit Kopniczky and Viktoria Hornok (University of Szeged) for the AFM measurements.\n
CAplus AN 2015:1013556; MEDLINE PMID: 26087390 (Journal; Article; Research Support, Non-U.S. Gov't);
AB  - Abstract In the course of our previous work, the interactions of two peptide fragments (GluR1201–230 and GluR1231–259) of human glutamate receptor (GluR1201–300) polypeptide with kynurenic acid (KYNA) were investigated by surface plasmon resonance (SPR) spectroscopy. Besides quantitation of the interactions, the enthalpies of binding of KYNA on certain peptide fragment-modified gold surfaces were also reported. In the present work, a third peptide fragment (GluR1270–300) of the glutamate receptor was synthesized and its interaction with KYNA was investigated by an SPR technique. This 31-membered peptide was chemically bonded onto a gold-coated SPR chip via a cysteine residue. The peptide-functionalized biosensor chip was analyzed by atomic force microscopy (AFM) and theoretical calculations were performed on the structure and dimensions of the peptide on the gold surface. In order to determine the isosteric heat of adsorption of the binding of KYNA on the peptide-functionalized gold thin film, SPR experiments were carried out between +10 °C and +40 °C. The results on the GluR1270–300–KYNA system were compared with the previously published binding parameters of the interactions of GluR1201–230 and GluR1231–259 with KYNA. The binding abilities of KYNA with all three peptide fragments immobilized on the gold surface were estimated by a molecular docking procedure and the binding free energies of these AMPA receptor subunits with KYNA were determined.
LA  - English
DB  - MTMT
ER  -