Pavlína Maloy Řezáčová

Structural Biology

We see every atom.

Knowledge of the three-dimensional structure of proteins responsible for cancer development plays a key role in the development of molecules with anticancer effects. Enzymes in particular are good targets for rational drug design as they have well-defined active sites for substrate binding and many have allosteric sites for regulatory binding. Structural information about the binding of a small molecule to a protein can be used for structure-inspired design of ligands. 

Among the enzymes whose expression and activity are associated with cancer development, human carbonic anhydrases and protein kinases, specifically carbonic anhydrase IX (CA IX) and cyclin-dependent kinases (CDK), are suitable targets for the development of specific inhibitors for use as anticancer drugs or diagnostics. The challenge is to prepare a compound that will selectively inhibit a particular isoform of these enzymes while keeping the affinity for others, and thus the potential side effects, to a minimum. We use the structural information to guide the design of such compounds.

SELECTED PUBLICATIONS
  • Brynda J, Mader P, Šícha V, Fábry M, Poncová K, Bakardiev M, Grüner B, Cígler P, Řezáčová P. Carborane-based carbonic anhydrase inhibitors. Angew Chem Int Ed Engl. 2013 Dec 16;52(51):13760-3. DOI: 10.1002/anie.201307583
  • Grüner B, Brynda J, Das V, Šícha V, Štěpánková J, Nekvinda J, Holub J, Pospíšilová K, Fábry M, Pachl P, Král V, Kugler M, Mašek V, Medvedíková M, Matějková S, Nová A, Lišková B, Gurská S, Džubák P, Hajdúch M, Řezáčová P. Metallacarborane Sulfamides: Unconventional, Specific, and Highly Selective Inhibitors of Carbonic Anhydrase IX. J Med Chem. 2019 Nov 14;62(21):9560-9575. DOI: 10.1021/acs.jmedchem.9b00945
  • Dvořanová J, Kugler M, Holub J, Šícha V, Das V, Nekvinda J, El Anwar S, Havránek M, Pospíšilová K, Fábry M, Král V, Medvedíková M, Matějková S, Lišková B, Gurská S, Džubák P, Brynda J, Hajdúch M, Grüner B, Řezáčová P. Sulfonamido carboranes as highly selective inhibitors of cancer-specific carbonic anhydrase IX. Eur J Med Chem. 2020 Aug 15;200:112460. DOI: 10.1016/j.ejmech.2020.112460
  • Skacel, J., Djukic, S., Baszczynski, O., Kalcic, F., Bilek, T., Chalupsky, K., Kozak, J., Dvorakova, A., Tloust’ova, E., Kral’ova, Z., Smidkova, M., Voldrich, J., Rumlova, M., Pachl, P., Brynda, J., Vuckova, T., Fabry, M., Snasel, J., Pichova, I., Rezacova, P., Mertlikova-Kaiserova, H. & Janeba, Z. (2023) Design, Synthesis, Biological Evaluation, and Crystallographic Study of Novel Purine Nucleoside Phosphorylase Inhibitors, J Med Chem. 25;66(10):6652-6681. DOI: 10.1021/acs.jmedchem.2c02097
SPECIALIZED EXPERTISE AND TECHNOLOGY

Macromolecular X-ray crystallography and NMR

Recombinant protein production

COLLABORATION WITH LARGE RESEARCH INFRASTRUCTURES AND RESEARCH CENTRES

Biotechnology and Biomedicine Centre of the Czech Academy of Sciences and the Charles University BIOCEV

Central European Institute of Technology at Masaryk University CEITEC MU