Mu.Ta.Lig - COST ACTION CA15135


5 December 2016

General information

Name: Asta
Surname: Zubrienė
Cell phone number with international prefix: +370 620 67249
Country: Lithuania
Affiliation: Vilnius university, Institute of Biotechnology, Department of Biothermodynamics and drug design
Gender: F
Year of the PhD title: 2003
Personal web page:
Previous COST participation: CA15126


List of 10 selected publications within last 5 years

1. Zubrienė A., Gutkowska M., Matulienė, J., et al. 2010. Thermodynamics of radicicol binding to human Hsp90 alpha and beta isoforms. Biophys. Chem. 152(1-3): 153-63
2. Rink C., Sasse F., Zubrienė A., Matulis D. and Maier M. E. 2010. Probing the influence of an allylic methyl group in zearlenone analogues on binding to Hsp90. Chem., Eur. J. 16, 14469-14478.
3. Čapkauskaitė E., Zubrienė A., Baranauskienė L., Tamulaitienė G., Manakova L., Kairys V., Gražulis S., Tumkevičius S., Matulis, D. 2012. Design of [(2-pyrimidinylthio)acetyl]benzenesulfonamides as inhibitors of human carbonic anhydrases. Eur. J. Med. Chem. 51: 259-270. ISSN: 0223-5234
4. Pirrie L., McCarthy A. R., Major L., Morkūnaitė, V., Zubrienė A., Matulis D., Lain S., Lebl T., Westwood N. J. 2012. Discovery and Validation of SIRT2 Inhibitors Based on Tenovin-6: Use of a H-NMR Method to Assess Deacetylase Activity. Molecules. 17: 12206-12224. ISSN: 1420-3049
5. Jogaitė V., Zubrienė A., Michailovienė V., Gylytė J., Morkunaitė V., Matulis D. 2013. Characterization of Human Carbonic Anhydrase XII Stability and Inhibitor Binding. Bioorg. Med. Chem. 21: 1431–1436
6. Zubrienė A., Čapkauskaitė E, Gylytė J., Kišonaitė M., Tumkevičius S, Matulis D. 2013. Benzenesulfonamides with benzimidazole moiety as inhibitors of carbonic anhydrases I, II, VII, XII and XIII. J. Enz. Inhib. Med. Chem. doi. 10.3109/14756366.2012.757223
7. Dudutienė V., Matulienė J., Smirnov, A., Timm, D., Zubrienė A., 2014. „Discovery and characterization of novel selective inhibitors of carbonic anhydrase IX“. J. Med. Chem. 57: 9435-9446.
8. Kišonaitė M., Zubrienė A., Čapkauskaitė E. 2014. Intrinsic thermodynamics and structure correlation of benzenesulfonamides with a pyrimidine moiety binding to carbonic anhydrases I, II, VII, XII, and XIII. PlosOne.  DOI:10.1371/journal.pone.0114106
9. Zubrienė A, Smirnovienė J., Smirnov A., Morkūnaitė V., Michailovienė V., Jachno J., Juozapaitienė V., Norvaišas P., Manakova E., Gražulis S., Matulis D. 2015. Intrinsic thermodynamics of 4-substituted-2,3,5,6-tetrafluorobenzenesulfonamide binding to carbonic anhydrases by isothermal titration calorimetry. Biophys. Chem. 205, 51-65.
10. Dudutienė V., Zubrienė A., Smirnov A., Timm D.D., et al. 2015. Functionalization of fluorinated benzenesulfonamides and their inhibitory properties toward carbonic anhydrases. ChemMedChem. 10: 662-687


Main skills and expertise (up to 5)

1. Biophysics of proteins, especially in the fields of protein-ligand interactions, protein folding and thermodynamics.
2. Biophysical and enzymatic methods used to analyze protein-ligand binding and inhibition (DSF, DSC, ITC, SPR)
3. Analysis of structure–energetics relationship in the enzyme ligand system.
4. Protein immobilization on various carriers


Main equipment/facilities available in the participants’ lab (up to 5)

1.      Isothermal titration calorimeters: vpITC, ITC200, Nano-ITC
2.      Real time PCR machine Corbett Rotor-Gene 6000, suitable for protein melting temperature determination.
3.      ISS PC1 photon counting spectrofluorimeter with integrated pressure pump for protein unfolding measuring at high pressures
4.      All necessary equipment for protein production in E.coli and mammalian cells, for protein purification, and chemical synthesis of compounds



Short personal activity proposal for the COST Action CA15135 (max 1000 characters)

Our laboratory is highly experienced in the field of organic synthesis, recombinant protein production, including cloning, production in bacterial and mammalian cultures, and biophysical measurements of compounds interaction with target proteins. To date we have a library of more than 700 sulfonamides, drug candidates for carbonic anhydrases and over 50 inhibitors of heat shock protein Hsp90. Our highly usable and universal biophysical approach, fluorescent thermal shift assay (differential scanning fluorimetry), can help to implement one of the COST tasks, to evaluate the ligands against selected multi-targets and determine protein-ligand binding affinity in a broad ranges of Kbs. Our group is also engaged in determining another thermodynamic properties such as enthalpy, entropy, heat capacity, volume, expansion and compressibility of interaction, which provide additional information on the molecular recognition phenomenon and rational drug design.


Work Group preference: score from 1 (preferred) to 4 (not preferred)

Work Group of the CA15135 COST Action Score
WG1: Development of new chemical entities 2
WG2: Selection of biological targets and assessment of biological data 1
WG3: Development of chemical databases 4
WG4: Development of Computational methods for multiple ligand design and discovery 3