Modelling and characterization of the sorption of kynurenic acid on protein surfaces

Ádám Juhász, Edit Csapó, L. Vécsei, I. Dékány

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

This paper presents a surface plasmon resonance (SPR) spectroscopy-based evaluation process which provides information on kinetic and thermodynamic aspects of the interactions between proteins and a drug molecule. Reversible binding of kynurenic acid (KYNA) on human (HSA) and bovine (BSA) serum albumin-modified gold sensor surface has been investigated under physiological conditions at various temperatures. The SPR sensorgrams were fitted via nonlinear parameter estimation method by using pseudo first order kinetic model. Based on the concentration dependence of the estimated observed rate constants (kobs) the association (ka) and dissociation (kd) constants as well as the equilibrium constants (KA) and the Gibbs free energy (ΔG0) change were calculated at different (10-35 C°) temperatures. Furthermore, the enthalpy (ΔH0), entropy (ΔS0) and heat capacity changes (ΔCp) of KYNA-protein complex formation were also calculated.

Original languageEnglish
Pages (from-to)3-9
Number of pages7
JournalPeriodica Polytechnica: Chemical Engineering
Volume61
Issue number1
DOIs
Publication statusPublished - 2017

Fingerprint

Kynurenic Acid
Surface plasmon resonance
Sorption
Membrane Proteins
Proteins
Kinetics
Acids
Equilibrium constants
Gibbs free energy
Serum Albumin
Gold
Parameter estimation
Specific heat
Enthalpy
Rate constants
Entropy
Association reactions
Spectroscopy
Thermodynamics
Temperature

Keywords

  • Binding kinetics
  • Enthalpy
  • Entropy
  • Heat capacity
  • Kynurenic acid
  • Serum albumins
  • Surface plasmon resonance spectroscopy
  • Van’t Hoff relation

ASJC Scopus subject areas

  • Chemical Engineering(all)

Cite this

Modelling and characterization of the sorption of kynurenic acid on protein surfaces. / Juhász, Ádám; Csapó, Edit; Vécsei, L.; Dékány, I.

In: Periodica Polytechnica: Chemical Engineering, Vol. 61, No. 1, 2017, p. 3-9.

Research output: Contribution to journalArticle

@article{ad078992ecb240649ace8a6fca9ebed7,
title = "Modelling and characterization of the sorption of kynurenic acid on protein surfaces",
abstract = "This paper presents a surface plasmon resonance (SPR) spectroscopy-based evaluation process which provides information on kinetic and thermodynamic aspects of the interactions between proteins and a drug molecule. Reversible binding of kynurenic acid (KYNA) on human (HSA) and bovine (BSA) serum albumin-modified gold sensor surface has been investigated under physiological conditions at various temperatures. The SPR sensorgrams were fitted via nonlinear parameter estimation method by using pseudo first order kinetic model. Based on the concentration dependence of the estimated observed rate constants (kobs) the association (ka) and dissociation (kd) constants as well as the equilibrium constants (KA) and the Gibbs free energy (ΔG0) change were calculated at different (10-35 C°) temperatures. Furthermore, the enthalpy (ΔH0), entropy (ΔS0) and heat capacity changes (ΔCp) of KYNA-protein complex formation were also calculated.",
keywords = "Binding kinetics, Enthalpy, Entropy, Heat capacity, Kynurenic acid, Serum albumins, Surface plasmon resonance spectroscopy, Van’t Hoff relation",
author = "{\'A}d{\'a}m Juh{\'a}sz and Edit Csap{\'o} and L. V{\'e}csei and I. D{\'e}k{\'a}ny",
year = "2017",
doi = "10.3311/PPch.10185",
language = "English",
volume = "61",
pages = "3--9",
journal = "Periodica Polytechnica: Chemical Engineering",
issn = "0324-5853",
publisher = "Budapest University of Technology and Economics",
number = "1",

}

TY - JOUR

T1 - Modelling and characterization of the sorption of kynurenic acid on protein surfaces

AU - Juhász, Ádám

AU - Csapó, Edit

AU - Vécsei, L.

AU - Dékány, I.

PY - 2017

Y1 - 2017

N2 - This paper presents a surface plasmon resonance (SPR) spectroscopy-based evaluation process which provides information on kinetic and thermodynamic aspects of the interactions between proteins and a drug molecule. Reversible binding of kynurenic acid (KYNA) on human (HSA) and bovine (BSA) serum albumin-modified gold sensor surface has been investigated under physiological conditions at various temperatures. The SPR sensorgrams were fitted via nonlinear parameter estimation method by using pseudo first order kinetic model. Based on the concentration dependence of the estimated observed rate constants (kobs) the association (ka) and dissociation (kd) constants as well as the equilibrium constants (KA) and the Gibbs free energy (ΔG0) change were calculated at different (10-35 C°) temperatures. Furthermore, the enthalpy (ΔH0), entropy (ΔS0) and heat capacity changes (ΔCp) of KYNA-protein complex formation were also calculated.

AB - This paper presents a surface plasmon resonance (SPR) spectroscopy-based evaluation process which provides information on kinetic and thermodynamic aspects of the interactions between proteins and a drug molecule. Reversible binding of kynurenic acid (KYNA) on human (HSA) and bovine (BSA) serum albumin-modified gold sensor surface has been investigated under physiological conditions at various temperatures. The SPR sensorgrams were fitted via nonlinear parameter estimation method by using pseudo first order kinetic model. Based on the concentration dependence of the estimated observed rate constants (kobs) the association (ka) and dissociation (kd) constants as well as the equilibrium constants (KA) and the Gibbs free energy (ΔG0) change were calculated at different (10-35 C°) temperatures. Furthermore, the enthalpy (ΔH0), entropy (ΔS0) and heat capacity changes (ΔCp) of KYNA-protein complex formation were also calculated.

KW - Binding kinetics

KW - Enthalpy

KW - Entropy

KW - Heat capacity

KW - Kynurenic acid

KW - Serum albumins

KW - Surface plasmon resonance spectroscopy

KW - Van’t Hoff relation

UR - http://www.scopus.com/inward/record.url?scp=85010809693&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85010809693&partnerID=8YFLogxK

U2 - 10.3311/PPch.10185

DO - 10.3311/PPch.10185

M3 - Article

AN - SCOPUS:85010809693

VL - 61

SP - 3

EP - 9

JO - Periodica Polytechnica: Chemical Engineering

JF - Periodica Polytechnica: Chemical Engineering

SN - 0324-5853

IS - 1

ER -