
The HUN-REN - ELTE Protein Modelling Research Group and the Structural Chemistry and Biology Laboratory are located at the Institute of Chemistry, Faculty of Natural Sciences, Eötvös Loránd University. We collaborate with many national and international structural research groups in various fields of organic- and peptide-chemistry, molecular biology and biochemistry to better understand the wonderful but hidden world of the microcosm. We operate and develop a synthetic platform including a system for the synthesis of polypeptides and protein domains based on flow chemistry, and a fermentor reactor for the production of partially unlabelled and partially 15N-and 13C-isotopically labelled proteins.
Our topics include spatially oriented projects such as foldamer research, understanding self-assembled and reversible amyloid formation, total synthesis of non-natural amino acids and sugar amino acids and chemical synthesis of polypeptides and protein domains. We also have projects to produce drugs and molecules as potential lead compounds related to diseases. These include a deeper understanding of the molecular basis of Alzheimer's disease, the kRas signalling protein that plays an important role in tumour diseases, the mechanism of antibiotics and a deeper understanding of certain drug-drug interactions. Our protein modelling work has also successfully addressed bioinformatics, molecular modelling, drug design and applied quantum chemistry challenges. Over the last decade, we have led several ELTE-centred collaborations and tenders to exploit the potential of important high-resolution structural tools such as NMR spectroscopy, X-ray crystallography and cryo-electron microscopy at the highest level and efficiently, to share our knowledge with others and to collaborate with industrial partners. (MedInProt, HunProtExc, or the Level Plus Programmes of Excellence, iNEXT-Discovery H-2020, etc.) Our open-minded, enthusiastic team welcomes students and is happy to cooperate with all interested researchers.

News
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Amide isomerization pathways II: Tracing geometrical prerequisites of acid-catalyzed amide cis–trans isomerization in globular proteins
In this article, with using MD simulations and statistical analysis of PDB structures, we identified favourable orientations of Asp/Glu carboxyl sidechains and water molecules, surrounding cis and trans peptide bonds in protein structures, satisfying the geometric criteria for the key steps of a previously proposed isomerization mechanism.
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TARPγ2-Derived Peptide Enhances Early-Phase Long-Term Potentiation and Impairs Memory Retention in Male Rats
Our new study shows that a short peptide derived from the TARPγ2 protein significantly influences synaptic plasticity in the brain: while it enhances early neural processes of learning, it simultaneously impairs later spatial memory retrieval in rats. These findings provide new insight into the molecular regulation of memory and may contribute to a better understanding of neurological disorders associated with altered synaptic function.
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The First Domestic Cryo-EM Platform Conference
On 14 February 2026, the HUN-REN TTK auditorium hosted the first national Cryo-electron microscopy conference, which marks a milestone in the history of structural biology in Hungary. Participants had the opportunity to learn about the Hungarian Cryo-EM Platform (HCEMP) equipment pool, which makes Hungarian science internationally competitive with state-of-the-art Krios and Glacios microscopes. The event highlighted that cryo-EM technology is not just a measurement method, but an innovative ecosystem shaping the future of precision medicine and materials science. The conference concluded with a message emphasising the power of collaboration: by sharing infrastructure and knowledge, Hungary has become an active shaper of the global molecular revolution.
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Recent Publications
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Dóra Soltész , Ildikó Szabó , Viktor Farkas , Nikolett Borók , Tamás Visnovitz , Dorina Lenzinger , Fülöp Károly Grébecz , Szilvia Bősze , Zoltán Bánóczi
Penetratin an Old Player in the Field of Cell-Penetrating Peptides Is in New Custom - Effect of Aromatic Non-Natural Amino Acid Substitutions
Pharmaceutics 18(5): 555 (2026) Kivonat -
István Bódy , Zsolt Fazekas , Nóra Wagner , Anna Kiss-Szemán , Veronika Harmat , Zoltán Pozsonyi , Dóra K. Menyhárd , András Perczel
Investigating transthyretin variants H88R and I107V in amyloid priming: From destabilization to complete dissociation
The FEBS Journal (2026) Kivonat -
Imola Cs. Szigyártó , Kristóf Ferentzi , András Wacha , Kamal el Battioui , Olivér Pavela , Vignesh Udyavara Nagaraj , Viktor Farkas , Tamás Beke-Somfai
Sequence-Driven Modulation of the Multistage Self-Assembly Process in Lamellin-Type β-Peptides
Aggregate 7(2): e70282 (2026) Kivonat -
Márton Gadanecz , Zsolt Fazekas , Dóra K. Menyhárd , András Perczel
Improving Protein Structure Determination by Integrating Ensemble-Driven Molecular Dynamics with Chemical Shift-Based Restraints
Journal of Chemical Information and Modeling 66(5): 2844 (2026) Kivonat -
Ádám A. Kelemen , András Perczel , Imre Jákli
Quantum Computing Simulations Elucidate Active Spaces and Energetics of Amide Bond Detailing the Cis-TS-Trans Isomerization
International Journal of Quantum Chemistry 126(4): e70160 (2026) Kivonat - More publications