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Department of Bioorganic Chemistry is one of 15 departments of Faculty of Chemistry, Wrocław University of Technology. It was founded in 1971 by Professor Przemysław Mastalerz in response to introduction of biochemistry and biotechnology curricula at Faculty of Chemistry. Now it is headed by Professor Paweł Kafarski and formed by 6 professors, 10 assistant professors and over 25 PhD students doing research on a border of chemistry and biology.


Members

Research

Publications


II Szkoła Chemii Bioorganicznej


Recent papers

The application of unnatural amino acids in protease probes
Maluch I, Czarna J, Drag M
Chemistry - An Asian Journal 2019, 1
DOI: 10.1002/asia.201901152

Recent papers

Tissue-ABPP enables high-resolution confocal fluorescence imaging of serine hydrolase activity in cryosections – Application to glioma brain unveils activity hotspots originating from tumor-associated neutrophils
Aaltonen N, Singha P, Jakupovic H, Wirth T, Samaranayake H, Pasonen-Seppanen S, Rilla K, Varjosalo M, Edgington-Mitchell L, Kasperkiewicz P, Drag M, Kalvala S, Moisio E, Savinainen JR, Laitinen JT
bioRxiv 2019, 1
DOI: 10.1101/783704

Recent papers

The Activome: multiplexed probing of activity of proteolytic enzymes using mass cytometry-compatible activity-based probes (TOF-probes)
Poreba M, Groborz K, Rut W, Pore M, Snipas SJ, Vizovisek M, Turk B, Drag M, Salvesen GS
bioRxiv 2019, 1
DOI: 10.1101/775627

Recent papers

Application of a chemical probe to detect neutrophil elastase activation during inflammatory bowel disease
Anderson BM, Poole DP, Aurelio L, Ng GZ, Fleischmann M, Kasperkiewicz P, Morissette C, Drag M, van Driel IR, Schmidt BL, Vanner SJ, Bunnett NW, Edgington-Mitchell LE
Scientific Reports 2019, 9, 13295
DOI: 10.1038/s41598-019-49840-4

Recent papers

Phosphonic Acid Analogues of Phenylglycine as Inhibitors of Aminopeptidases: Comparison of Porcine Aminopeptidase N, Bovine Leucine Aminopeptidase, Tomato Acidic Leucine Aminopeptidase and Aminopeptidase from Barley Seeds
Wanat, W.; Talma, M.; Pawełczak, M.; Kafarski, P.
Pharmaceuticals 2019, 12, 1
DOI: 10.3390/ph12030139

Abstract
The inhibitory activity of 14 racemic phosphonic acid analogs of phenylglycine, substituted in aromatic rings, towards porcine aminopeptidase N (pAPN) and barley seed aminopeptidase was determined experimentally. The obtained patterns of the inhibitory activity against the two enzymes were similar. The obtained data served as a basis for studying the binding modes of these inhibitors by pAPN using molecular modeling. It was found that their aminophosphonate fragments were bound in a highly uniform manner and that the difference in their affinities most likely resulted from the mode of substitution of their phenyl rings. The obtained binding modes towards pAPN were compared, with these predicted for bovine lens leucine aminopeptidase (blLAP) and tomato acidic leucine aminopeptidase (tLAPA). The performed studies indicated that the binding manner of the phenylglycine analogs to biLAP and tLAPA are significantly similar and di er slightly from that predicted for pAPN.

Recent papers

Botanical Origin Authentication of Polish Phacelia Honey Using the Combination of Volatile Fraction Profiling by HS‑SPME and Lipophilic Fraction Profiling by HPTLC
Makowicz, E.; Jasicka-Misiak, I.; Teper, D.; Kafarski, P.
Chromatographia 2019, 82, 1541
DOI: 10.1007/s10337-019-03778-x

Abstract
Eleven samples of Polish Phacelia tanacetifolia Benth., three Brassica napus and one Salix spp. honeys were characterized by melissopalynology and analysis of the compositions of their volatile fractions. Headspace solid-phase microextraction coupled with gas chromatography mass spectrometry (HS-SPME/GC–MS) using PDMS/CAR/DVB fiber was used for the isolation of low-molecular weight compounds which create a volatile fraction. To differentiate and indicate the most representative unifloral samples, chemometric techniques such as principal component analysis (PCA) and hierarchical-tree clustering (HTC) were applied to the dataset of the chromatographic fingerprints. Based on the obtained results, a unique chemical fingerprint of phacelia honey was generated. This study allows us to discriminate the botanical origin of the phacelia honeys based on the GC–MS and HPTLC analysis. In case of the GC–MS analysis trans-linalool oxide, hotrienol, cislinalool oxide and cis-epoxylinalool were identified as a predominant compound. Additionally lipophilic fractions obtained by ultrasound-assisted extraction (UAE) and solid-phase extraction (SPE) were subjected to the HPTLC analysis. It allowed the construction of a barcode-type identifier that could be used to differentiate the honey samples even without identifying the individual components of the obtained fraction.

Recent papers

Synthesis and conformational preferences of short analogues of antifreeze glycopeptides (AFGP)
Urbańczyk M., Jewgiński M, Krzciuk-Gula J., Góra J., Latajka R., Sewald N.
Beilstein J. Org. Chem. 2019, 15, 1581
DOI: 10.3762/bjoc.15.162
Abstract
Antifreeze glycoproteins are a class of biological agents which enable living at temperatures below the freezing point of the body fluids. Antifreeze glycopeptides usually consist of repeating tripeptide unit (-Ala-Ala-Thr*-), glycosylated at the threonine side chain. However, on the microscopic level, the mechanism of action of these compounds remains unclear. As previous research has shown, antifreeze activity of antifreeze glycopeptides strongly relies on the overall conformation of the molecule as well an on the stereochemistry of amino acid residues. The desired monoglycosylated analogues with acetylated amino termini and the carboxy termini in form of N-methylamide have been synthesized. Conformational nuclear magnetic resonance (NMR) studies of the designed analogues have shown a strong influence of the stereochemistry of amino acid residues on the peptide chain stability, which could be connected to the antifreeze activity of these compounds. A better understanding of the mechanism of action of antifreeze glycopeptides would allow applying these materials, e.g., in food industry and biomedicine.

Recent papers

Leveraging peptide substrate libraries to design inhibitors of bacterial Lon protease
Babin BM, Kasperkiewicz P, Janiszewski T, Yoo E, Drag M, Bogyo M
ACS Chemical Biology 2019, 1
DOI: 10.1021/acschembio.9b00529

Recent papers

Fluorescent activity-based probe for the selective detection of Factor VII activating protease (FSAP) in human plasma
Rut W, Nielsen NV, Czarna J, Poreba M, Kanse SM, Drag M
Thrombosis Research 2019, 1
DOI: 10.1016/j.thromres.2019.08.016

Recent papers

Fluorescent probes towards selective cathepsin B detection and visualization in cancer cells and patient samples
Poreba M, Groborz K, Vizovisek M, Maruggi M, Turk D, Turk B, Powis G, Drag M, Salvesen GS
Chemical Science 2019, 1
DOI: 10.1039/C9SC00997C