General information

Name: Lina

Surname: Baranauskiene

E-mail: linami@ibt.lt     lina.baranauskiene@bti.vu.lt

Cell phone number with international prefix: +37064501172

Country: Lithuania

Affiliation: Institute of Biotechnology, Vilnius University

Gender: F

Year of the PhD title: 2013

Personal web page: http://

Previous COST participation: No

 

List of 10 selected publications within last 5 years

1. Identification of a small-molecule ligand of the epigenetic reader protein Spindlin1 via a versatile screening platform. Wagner T, Greschik H, Burgahn T, Schmidtkunz K, Schott AK, McMillan J, Baranauskiene L, Xiong Y, Fedorov O, Jin J, Oppermann U, Matulis D, Schüle R, Jung M. Nucleic Acids Res. 2016 Feb 17. pii: gkw089.

2. Looking for a generic inhibitor of amyloid-like fibril formation among flavone derivatives. Šneideris T, Baranauskiene L, Cannon JG, Rutkiene R, Meškys R, Smirnovas V. PeerJ. 2015 Sep 24;3:e1271. doi: 10.7717/peerj.1271.

3. Discovery and characterization of novel selective inhibitors of carbonic anhydrase IX. Dudutiene V, Matuliene J, Smirnov A, Timm DD, Zubriene A, Baranauskiene L, Morkūnaite V, Smirnoviene J, Michailoviene V, Juozapaitiene V, Mickevičiūte A, Kazokaite J, Bakšyte S, Kasiliauskaite A, Jachno J, Revuckiene J, Kišonaite M, Pilipuityte V, Ivanauskaite E, Milinavičiūte G, Smirnovas V, Petrikaite V, Kairys V, Petrauskas V, Norvaišas P, Linge D, Gibieža P, Capkauskaite E, Zakšauskas A, Kazlauskas E, Manakova E, Gražulis S, Ladbury JE, Matulis D. J Med Chem. 2014 Nov 26;57(22):9435-46. doi: 10.1021/jm501003k.

4. Saccharin sulfonamides as inhibitors of carbonic anhydrases I, II, VII, XII, and XIII. Morkūnaite V, Baranauskiene L, Zubriene A, Kairys V, Ivanova J, Trapencieris P, Matulis D. Biomed Res Int. 2014;2014:638902. doi: 10.1155/2014/638902.

5. Intrinsic thermodynamics of sulfonamide inhibitor binding to human carbonic anhydrases I and II. Morkūnaite V, Gylyte J, Zubriene A, Baranauskiene L, Kišonaite M, Michailoviene V, Juozapaitiene V, Todd MJ, Matulis D. J Enzyme Inhib Med Chem. 2015 Apr;30(2):204-11. doi: 10.3109/14756366.2014.908291.

6. Intrinsic thermodynamics of ethoxzolamide inhibitor binding to human carbonic anhydrase XIII. Baranauskiene L, Matulis D. BMC Biophys. 2012 Jun 7;5:12. doi: 10.1186/2046-1682-5-12.

7. Design of [(2-pyrimidinylthio)acetyl]benzenesulfonamides as inhibitors of human carbonic anhydrases. Čapkauskaite E, Zubriene A, Baranauskiene L, Tamulaitiene G, Manakova E, Kairys V, Gražulis S, Tumkevičius S, Matulis D. Eur J Med Chem. 2012 May;51:259-70. doi: 10.1016/j.ejmech.2012.02.050.

8. Indapamide-like benzenesulfonamides as inhibitors of carbonic anhydrases I, II, VII, and XIII. Čapkauskaite E, Baranauskiene L, Golovenko D, Manakova E, Gražulis S, Tumkevičius S, Matulis D. Bioorg Med Chem. 2010 Nov 1;18(21):7357-64. doi: 10.1016/j.bmc.2010.09.016.

9. 4-[N-(substituted 4-pyrimidinyl)amino]benzenesulfonamides as inhibitors of carbonic anhydrase isozymes I, II, VII, and XIII. Sūdžius J, Baranauskiene L, Golovenko D, Matuliene J, Michailoviene V, Torresan J, Jachno J, Sukackaite R, Manakova E, Gražulis S, Tumkevičius S, Matulis D. Bioorg Med Chem. 2010 Nov 1;18(21):7413-21. doi: 10.1016/j.bmc.2010.09.011

10. Inhibition and binding studies of carbonic anhydrase isozymes I, II and IX with benzimidazo[1,2-c][1,2,3]thiadiazole-7-sulphonamides. Baranauskiene L, Hilvo M, Matuliene J, Golovenko D, Manakova E, Dudutiene V, Michailoviene V, Torresan J, Jachno J, Parkkila S, Maresca A, Supuran CT, Gražulis S, Matulis D. J Enzyme Inhib Med Chem. 2010 Dec;25(6):863-70. doi: 10.3109/14756360903571685.

 

Main skills and expertise (up to 5)

1. Analysis of protein-ligand binding using biophysical techniques (ITC, FTSA)

2. Analysis of protein stability, selection of buffers/additives (FTSA, DSC)

3. Analysis of protein amyloid aggregation.

4. Analysis of enzymatic activity using stopped-flow technique.

5. Common cloning, protein expression (in bacteria) and purification methods.

 

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

1. Isothermal titration calorimeters (iTC200, VP-ITC)

2. Qiagen qPCR machine with blue channel (used for fluorescent thermal shift assay)

3. Standard equipment for cloning, protein production in bacteria and mammalian cell lines , protein purification, chemical synthesis

 

 

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

One of the tasks in this COST action is to design novel or identify existing bioactive compounds, which could interact selectively with two or more macromolecular targets. As every target protein has its own catalytic or other biological activity, different activity evaluation tests are used to identify interacting compounds. Versatility of biophysical interaction methods could be employed both for primary screening and ligand affinity ranking. Our laboratory can propose fluorescence based thermal shift assay (also known as differential scanning fluorimetry), which enables quick selection of interacting small molecules according to changes in protein stability (melting temperature). It can be used to detect binding in very wide affinity range. Presently we are working with target proteins: carbonic anhydrases (we have all 12 catalytically active proteins), Hsp90 (alpha and beta isoforms), and several others (HDAC8, sirtuin2, etc.).

 

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