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Department of Bioorganic Chemistry

Katarzyna Ożga

ozga2.jpg

Born: August 24th, 1991

Room: 321b, building A2

Phone: +48 71 320 40 80

e-mail: katarzyna.ozga@pwr.edu.pl

Hobby: food and wine

ORCID: 0000-0002-2837-283X

Scopus ID: 57451399000


Research

  • 2022 principal investigator in ‘Utilization of π-cation stabilized β-hairpin for construction of hybrid tertiary structures’ (grant NCN Miniatura 2022/06/X/ST4/00008)
  • 2020 coinvestigator in ‘Peptide foldamer-based inhibitors of human ACE2 – SARS-CoV-
    2 S protein interaction’ (grant Fast Track COVID-19 no 2020/01/0/ST4/00064)
  • 2020-2021 contract coinvestigator in ‘De novo designed, structurally extended peptide
    foldamers and their use for construction of PD-1/PD-L1 interaction inhibitors’ (grant NCN Opus16
    no. 2018/31/B/ST5/02631)
  • 2017-2019 contract investigator in ‘Foldameric miniproteins - structure and catalytic
    function’ (grant NCN OPUS11 no. 2016/21/B/ST5/00269)
  • 2015-2017 contract investigator in ‘Artificial enzymes based on foldamers’ (grant NCN
    SONATA BIS3 no. 2013/10/E/ST5/00625)

Education

2015-2019 PhD in Chemistry, Wroclaw University of Science and Technology, Thesis title: Peptide foldamers with aldolase-like activity

2013-2015 MSc in Bioinformatics (in English)

2010-2013 Engineer in Biotechnology

Publications

1. Ożga, K.; Berlicki, Ł. Miniprotein-based artificial retroaldolase. ACS Catalysis
2. Ożga, K.; Berlicki, Ł. Design and Engineering of Miniproteins. ACS Bio Med Chem Au, 2022, DOI:
10.1021/acsbiomedchemau.2c00008.
3. Szefczyk, M.; Ożga, K.; Drewniak-Świtalska, M.; Rudzińska-Szostak, E., Hołubowicz, R.; Ożyhar, A.;
Berlicki, Ł. Controlling the conformational stability of coiled-coil peptides by a single stereogenic
center of peripheral β-amino acid residue. RSC Adv. RSC Adv., 2022, 12, 4640.
4. Stanojlovic, V.; Müller, A.; Moazzam, A.; Hinterholzer, A.; Ożga, K.; Berlicki, Ł.; Schubert, M.;
Cabrele, C. A Conformationally Stable Acyclic β-Hairpin Scaffold Tolerating the Incorporation of
Poorly β-Sheet-Prone Amino Acids. ChemBioChem 2021, 22, e2021006.
5. Grelich-Mucha, M.; Garcia, A.; Torbeev, V.; Ozga, K.; Berlicki, Ł.; Olesiak-Banska, J.
Autofluorescence of amyloids determined by enantiomeric composition of peptides. J. Phys.
Chem. B 2021, 125, 5502–5510.
6. Ożga, K.; Drewniak-Świtalska, M.; Rudzińska-Szostak, E.; Berlicki, Ł., Towards Foldameric
Miniproteins: A Helix‐Turn‐Helix Motif. ChemPlusChem 2021, 86, 646–649.
7. Fortuna, P.; Twarda-Clapa, A.; Skalniak, L.; Ożga, K.; Holak, T. A.; Berlicki, Ł., Systematic
‘foldamerization’ of peptide inhibiting p53-MDM2/X interactions by the incorporation of trans- or
cis-2-aminocyclopentanecarboxylic acid residues. Eur. J. Med. Chem. 2020, 208, 112814.
8. Drewniak, M.; Węglarz-Tomczak, E.; Ożga, K.; Rudzińska-Szostak, E.; Macegoniuk, K.; Tomczak, J.
M.; Bejger, M.; Rypniewski, W.; Berlicki, Ł., Helix-loop-helix peptide foldamers and their use in the
construction of hydrolase mimetics. Bioorg. Chem. 2018, 81, 356.
9. Kolonko, M.; Ożga, K.; Hołubowicz, R.; Taube, M.; Kozak, M.; Ożyhar, A.; Greb-Markiewicz, B.
Intrinsic Disorder of the C-Terminal Domain of Drosophila Methoprene-Tolerant Protein. PLoS
One. 2016, 1, e0162950.

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