György Mády
Hungarian Academy of Sciences
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Featured researches published by György Mády.
Biochimica et Biophysica Acta | 2010
Ilona Fitos; Júlia Visy; Miklós Simonyi; György Mády; Ferenc Zsila
BACKGROUND alpha(1)-Acid glycoprotein (AGP) plays a decisive role in the serum protein binding of several drugs.Genetic variants of AGP have different ligand binding properties. The binding of deramciclane (DER), a chiral anxiolytic agent, has been studied on A and F1/S genetic variants of AGP. METHODS The effects of DER and reference drugs on the binding of specific fluorescent and circular dichroism (CD) probes of AGP were determined. Dicumarol (DIC) binding was measured by CD and equilibrium dialysis. RESULTS DER effectively displaced probes bound to variant A, while it was less effective at displacing probes bound to variant F1/S. DER increased the binding and inverted the induced CD spectrum of DIC in the solution of variant F1/S. This phenomenon could not be brought about by the enantiomer of DER. CONCLUSION DER has high-affinity binding (K(a)> or =2x10(6) M(-1)) to variant A, while its binding to the variant F1/S is about thirty times weaker. During simultaneous binding of DER and DIC to variant F1/S a ternary complex having about four times higher affinity is formed, in which the opposite chiral conformation of DIC is favored. GENERAL SIGNIFICANCE The binding interactions found prove that AGP can simultaneously accommodate different ligand molecules. Even weakly bound ligands can provoke unexpected allosteric protein binding interactions.
Rapid Communications in Mass Spectrometry | 1996
Zoltán Szilágyi; G Vas; György Mády; Károly Vékey
Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry was applied to the characterization of the protein content of wines. It has been established that this technique is applicable for this purpose even without sophisticated sample preparation. Direct structural information—presence of glycoproteins—was obtained from the MALDI spectra and was supported by an enzymatic degradation experiment. On the basis of the MALDI spectra it was possible to distinguish two different wines and a correlation was found between peak intensity ratios and the time of harvest.
International Journal of Biological Macromolecules | 2012
Ilona Fitos; Ágnes Simon; Ferenc Zsila; György Mády; Á Bencsura; Z. Varga; L. orfi; G. Kéri; Júlia Visy
Imatinib (IMT) is a selective tyrosine kinase inhibitor, used in the treatment of chronic myeloid leukemia and gastrointestinal stromal tumors. Its strong plasma protein binding was found to belong to the F1*S genetic variant of α(1)-acid glycoprotein (AGP). In this work, comparative AGP binding studies were performed with IMT fragment molecules to reveal which parts of the molecule are important in the high-affinity interaction provoking specific spectral changes. Molecular modeling calculations indicated that IMT docked into the X-ray structure of AGP/F1 adopts a bent, compact conformation. This binding mode is similar to those found in its complexes with some low-affinity kinases and a quinone reductase, being strikingly different from the extended conformation of IMT in its high-affinity kinase targets.
Biochemical Pharmacology | 2004
Ilona Fitos; Júlia Visy; Ferenc Zsila; Zsolt Bikádi; György Mády; Miklós Simonyi
Bioorganic & Medicinal Chemistry | 2008
Ferenc Zsila; Júlia Visy; György Mády; Ilona Fitos
Enantiomer | 2002
Zsolt Bikádi; Ferenc Zsila; József Deli; György Mády; Miklós Simonyi
Bioorganic & Medicinal Chemistry | 2007
Ilona Fitos; Júlia Visy; Ferenc Zsila; György Mády; Miklós Simonyi
Biochemical and Biophysical Research Communications | 2008
Ferenc Zsila; György Mády
Chirality | 2002
Júlia Visy; Ilona Fitos; György Mády; László Ürge; Péter Krajcsi; Miklós Simonyi
Biochimica et Biophysica Acta | 2008
Ferenc Zsila; Zsolt Bikádi; Eszter Hazai; Ágnes Simon; Ilona Fitos; György Mády