in spectra

NMR, ECD,

VCD, FTIR,..

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in crystal

 X-ray diffraction,

crystallography,...

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in silico

bio-informatics, applied QM,

molecular modeling,...

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in vivo/in vitro

biotechnology, protein production, 

preparative work, classical synthesis,..

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Csoport 2024.Aprilis

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.

P1030653

Csoport 1


News

  • Unveiling the Oxazolidine Character of Pseudoproline Derivatives by Automated Flow Peptide Chemistry

    Pseudoproline derivatives, like Thr(ΨPro)-OH, are utilized in peptide synthesis to minimize peptide aggregation and aspartimide formation, but they may induce notable side reactions, particularly under elevated temperature and pressure.This study explores the oxazolidine moiety's behavior and proposes mechanisms to mitigate these side reactions, offering a thermodynamically controlled solution to aspartimide formation.

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  • Intramolecular Inhibition by Imidazole in Acid-Catalyzed Hydrolysis of Protected Carbohydrates

    The study uncovers an anomaly in the acid-catalyzed hydrolysis of the 5,6-O-isopropylidene group in specific D-gluco- and D-allofuranose derivatives, linked to C3-epimers with 3-O-imidazole sulfonyl moieties. Advanced modeling reveals how interactions between protecting groups and steric effects inhibit this reaction, providing new insights into carbohydrate chemistry.

    Kép1

  • Direct Continuous Flow Synthesis of Two Difficult Polypeptides Using β-Cyclodextrins

    Cyclodextrins, particularly OH-free β-CyD, significantly reduce peptide aggregation during SPPS, enhancing the synthesis of challenging peptides like amyloid β (1-42). This innovative approach improves crude peptide purity by 8%-19%, offering an alternative to traditional pseudoproline monomer methods.

    Kép1

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Recent Publications