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
| Autor: | Imre Dékány, G.K. Tóth, Ádám Juhász, Zsófia Majláth, Ferenc Bogár, Dániel Sebők, László Vécsei, J. Szolomájer, Edit Csapó |
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| Rok vydání: | 2015 |
| Předmět: |
chemistry.chemical_classification
Chemistry Stereochemistry Peptide Surfaces and Interfaces General Medicine AMPA receptor Surface Plasmon Resonance Kynurenic Acid Microscopy Atomic Force Residue (chemistry) chemistry.chemical_compound Colloid and Surface Chemistry Adsorption Kynurenic acid Receptors Glutamate Biophysics Humans Physical and Theoretical Chemistry Surface plasmon resonance Biosensor Biotechnology Cysteine |
| Zdroj: | Colloids and Surfaces B: Biointerfaces. 133:66-72 |
| ISSN: | 0927-7765 |
| DOI: | 10.1016/j.colsurfb.2015.04.044 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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