General information
| Name: Pavla |
| Surname: Bojarová |
| E-mail: bojarova@biomed.cas.cz |
| Cell phone number with international prefix: +420-296442510 |
| Country: Czech Republic |
| Affiliation: Institute of Microbiology, Czech Academy of Sciences |
| Gender: F X M □ |
| Year of the PhD title: 2006 |
| Personal web page: http://www.biotrans.cas.cz/staff/ |
| Previous COST participation: No □ Yes X |
List of 10 selected publications within last 5 years
| 1. H. Ryšlavá, A. Kalendová, V. Doubnerová, P. Skočdopol, V. Kumar, Z. Kukačka, P. Pompach, O. Vaněk, K. Slámová, P. Bojarová, N. Kulik, R. Ettrich, V. Křen, K. Bezouška: Enzymatic characterization and molecular modeling of an evolutionarily interesting fungal b-N-acetylhexosaminidase. FEBS J. 2011, 278, 2469-2484. |
| 2. P. Bojarová, K. Slámová, K. Křenek, R. Gažák, N. Kulik, R. Ettrich, H. Pelantová, M. Kuzma, S. Riva, D. Adámek, K. Bezouška, V. Křen: Charged Hexosaminides as New Substrates for b-N-Acetylhexosaminidase-Catalyzed Synthesis of Immunomodulatory Disaccharides. Adv. Synth. Catal. 2011, 353, 2409-2420. |
| 3. C. Rech, R. R. Rosencrantz, K. Křenek, H. Pelantová, P. Bojarová, C. E. Römer, F. G. Hanisch, V. Křen, L. Elling: Combinatorial One-Pot Synthesis of Poly-N-acetyllactosamine Oligosaccharides with Leloir-Glycosyltransferases. Adv. Synth. Catal. 2011, 353, 2492-2500. |
| 4. Drozdová, P. Bojarová, K. Křenek, L. Weignerová, B. Henssen, L. Elling, H. Christensen, H. H. Jensen, H. Pelantová, M. Kuzma, K. Bezouška, M. Krupová, D. Adámek, K. Slámová, V. Křen: Enzymatic synthesis of dimeric glycomimetic ligands of NK cell activation receptors. Carbohydr. Res. 2011, 346, 1599-1609. |
| 5. K. Slámová, P. Bojarová, D. Gerstorferová, B. Fliedrová, J. Hofmeisterová, M. Fiala, P. Pompach, V. Křen: Sequencing, cloning and high-yield expression of a fungal β-N-acetylhexosaminidase in Pichia pastoris. Prot. Express. Purif. 2012, 82, 212-217. |
| 6. T. Desmet, W. Soetaert, P. Bojarová, V. Křen, L. Dijkhuizen, V. Eastwick-Field, A. Schiller: Enzymatic glycosylation of small molecules: Challenging substrates require tailored catalysts. Chem. Eur. J. 2012, 18, 10786–10801. |
| 7. H. Mrázek, L. Weignerová, P. Bojarová, P. Novák, O. Vaněk, K. Bezouška: Carbohydrate synthesis and biosynthesis technologies for cracking of the glycan code: Recent advances. Biotechnol. Adv., 2013, 31, 17-37. |
| 8. P. Bojarová, R. R. Rosencrantz, L. Elling, V. Křen: Enzymatic glycosylation of multivalent scaffolds. Chem. Soc. Rev. 2013, 42, 4774-4797. |
| 9. A. Šimonová, C. E. Kupper, S. Böcker, A. Müller, K. Hofbauerová, H. Pelantová, L. Elling, V. Křen, P. Bojarová: Chemo-enzymatic synthesis of LacdiNAc dimers of varying length as novel galectin ligands. J. Mol. Catal. B: Enzym., 2014, 101, 47-55. |
| 10. P. Bojarová, V. Křen: Sugared biomaterials binding lectins: achievements and perspectives. Biomater. Sci., 2016, DOI: 10.1039/c6bm00088f. |
Main skills and expertise (up to 5)
| 1. Chemoenzymatic and enzymatic carbohydrate synthesis |
| 2. Enzymology and protein chemistry |
| 3. Molecular biology – genetic engineering, cloning and expression |
| 4. Polymer chemistry |
| 5. Biological studies |
Main equipment/facilities available in the participants’ lab (up to 5)
| 1. HPLC-MS, analytical and preparative HPLCs |
| 2. Äkta Purifier, Äkta FPLC, Äkta Prime plus devices for protein purification |
| 3. 400, 600 and 700 MHz NMR devices |
| 4. Bruker APEX-Q FTMS, Finnigan LCQ-DECA, and Bruker BIFLEX II mass spectrometers |
| 5. Equipment for biochemistry, molecular biology, protein chemistry and cultivation of microorganisms |
Short personal activity proposal for the COST Action CA15135 (max 1000 characters)
| Our group is involved in the synthesis, study and biological evaluation of multivalent glycoconjugates with affinity to galectins, especially to Gal-3. Prospective multivalent epitopes have been prepared based on poly-LacNAc glycans and chito-oligomers. They are efficiently synthesized through chemo-enzymatic approach using a biocatalytical toolbox of recombinant wild-type and mutant glycosyltransferases, glycosidases and transglycosidases.
Prepared glycan structures are immobilized via suitable linkers to functionalized biomaterials, to ensure necessary multivalent display of epitopes. The conjugates, coupled with fluorescent tags for bio-imaging and/or with attached bioactive substances, are perfect enabling tools for targeted delivery: the destination is indicated by the display of target lectins, which bind the glycans presented on the biomaterial probe. Targeting with glyco-biomaterials shows enhanced efficacy, safety, biocompatibility, and selectivity. LacNAc- and LacdiNAc-derived structures may be directed, e.g., to Gal-3-overexpressing tumor tissue. The affinity of new glycomaterials to particular lectins and lectin-rich structures will be characterized using in vitro assays, cellular assays or robotic high-throughput-screening.
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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 | 3 |
| WG4: Development of Computational methods for multiple ligand design and discovery | 4 |
