Head: Dr. Gyula Tircsó
Teaching staff involved in the programme:
- Zsolt Baranyai
- Ernő Brücher
- Péter Buglyó
- Éva Dóka
- Etelka Farkas
- Zoltán Garda
- István Jószai
- Csilla Kállay
- Ferenc Krisztián Kálmán
- Nigel John Mason
- Péter Nagy
- Imre Sóvágó
- Dezső Szikra
- Gyula Tircsó
- Imre Tóth
- Katalin Várnagy
Research topics
Coordination chemistry research in bioinorganic chemistry. Complexes of metal ions of importance in medical diagnosis and therapy formed with oxygen- and nitrogen-donor polyfunctional ligands. Organometallic chemistry. Investigation of redox reactions that play a pivotal role in living organisms.
Description of the Doctoral Programme
Within the framework of the program, the largest area of the coordination chemistry research is dedicated to topics motivated by bioinorganic chemistry. One of the most extensive research fields involves the equilibrium and structural (UV–Vis, CD, ESR, NMR, MS) studies of complexes formed between essential trace elements (Fe, Cu, Zn, Ni, Co, Mn, Mo), as well as certain toxic elements (Cd, Pb, Pd), and amino acids, peptides, and their derivatives. In addition, the research also focus on the redox properties of the formed complexes, and on the metal ion–catalyzed oxidation and hydrolysis of peptides. The primary aim of these studies is to uncover potential relationships between metal ions and neurodegenerative disorders.
Another major area of coordination chemistry research concerns the thermodynamic, kinetic (formation, dissociation, solvent exchange, etc.) and structural characterization of complexes formed by oxygen- and nitrogen-donor polyfunctional ligands with metal ions used in medical diagnostics (e.g., Gd(III), Mn(II), Fe(II/III)) and in therapeutic applications, particularly metal isotopes (⁴⁷Sc, ⁶⁷Cu, ⁹⁰Y, ¹⁷⁷Lu, ²¹²Bi, ²²³Ra, ²²⁵Ac, etc.), as well as isotope pairs applicable in theragnostic procedures, combining diagnostic and therapeutic modalities (e.g., ⁴⁴/⁴⁷Sc, ⁶⁴/⁶⁷Cu, ⁸⁶/⁹⁰Y, ⁸⁹Zr/⁹⁰Y, ⁸⁹Zr/¹⁷⁷Lu, etc.). Based on the results of intensive research in these areas, our objectives also include the application-oriented design and synthesis of chelators and the characterization of their complexes - steps that are indispensable precursors to clinical applications. Recently, we have also turned our attention to the design and synthesis of “smart” probes (e.g., pH- or Zn(II)-responsive systems), organ-specific (e.g., liver-specific), and bimodal (MRI–PET, MRI–optical, etc.) contrast agent candidates. Techniques applied include pH-potentiometry (equilibrium studies), UV–visible spectrophotometry (equilibrium and kinetic measurements), spectrofluorimetry (equilibrium and kinetic studies), one- and multidimensional and TD NMR spectroscopy (using conventional nuclei such as ¹H, ¹³C, ¹⁷O, ¹⁹F and ³¹P, as well as more exotic nuclei such as ⁴⁵Sc, ⁶⁷Ga, ⁸⁹Y, ¹¹⁵In, ¹⁹⁵Pt, ²⁰³/²⁰⁵Tl, etc. for equilibrium, structural, kinetic, and dynamic studies), along with HPLC (analytical and preparative purification) and MS techniques supporting preparative organic chemistry (ligand synthesis).
Redox reactions play a fundamental role in living organisms. A substantial shift in the redox balance toward oxidative processes leads to oxidative distress, which is cell-damaging and may contribute to, among other things, the development of cancer. Reactive oxygen species (ROS), such as the superoxide radical anion (O2●-) and hydrogen peroxide (H₂O₂), are primarily responsible for oxidative stress. Therefore, the program places special emphasis on studying the oxidative processes induced by ROS on the thiol side chain of proteins containing cysteine (Cys-SH) amino acid residues (Protein–Cys–SH). These include investigating the effects of thiol-group redox reactions on protein function (inhibition or activation), protein–protein interactions, intracellular localization of proteins, and transcription-level regulation. Redox regulation - regulation via oxidation - affects numerous key proteins within cells, such as phosphatases, kinases, and various transcription factors. In this context, and from the perspective of redox signaling, H₂O₂ is the most important and widely studied oxidant. Consequently, our research objectives also include the detailed investigation of the enzymes responsible for its degradation, particularly the peroxiredoxin protein family. The study of reactive sulfur species (RSS) has become a significant field in redox biology in recent decades; their investigation is also within our scope, as are the persulfidation processes of redox-active proteins, given that reactive sulfur species play key roles both in tumor development and in the response to cancer therapy.