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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.


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Research

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News

Open positions for PhD student and Postdoc to work at project "Foldameric miniproteins - structure and catalytic function".

Konkurs na stypendium dla doktoranta oraz na stanowisko asystenta naukowego do pracy przy projekcie "Minibiałka forldamerowe - struktura i funkcja katalityczna".


Recent papers

Biodiversity in targeted metabolomics analysis of filamentous fungal pathogens by 1H NMR-based studies
Ząbek A, Klimek-Ochab M, Jawień E, Młynarz P
World J Microbiol Biotechnol 2017, 33, 132
DOI: DOI 10.1007/s11274-017-2285-7

Recent papers

Self-Assembled Protein-Aromatic Foldamer Complexes with 2:3 and 2:2:1 Stoichiometries
Jewginski, M., Granier, T., Langlois D’Estaintot, B., Fischer, L., Mackereth, C.D., Huc, I
Journal of the American Chemical Society 2017, 139, 2928
DOI: 10.1021/jacs.7b00184

Abstract
The promotion of protein dimerization using the aggregation properties of a protein ligand was explored and shown to produce complexes with unusual stoichiometries. Helical foldamer 2 was synthesized and bound to human carbonic anhydrase (HCA) using a nanomolar active site ligand. Crystal structures show that the hydrophobicity of 2 and interactions of its side chains lead to the formation of an HCA2-23 complex in which three helices of 2 are stacked, two of them being linked to an HCA molecule. The middle foldamer in the stack can be replaced by alternate sequences 3 or 5. Solution studies by CD and NMR confirm left-handedness of the helical foldamers as well as HCA dimerization.

Recent papers

A toolbox of fluorescent probes for parallel imaging reveals uneven location of serine proteases in neutrophils
Kasperkiewicz P, Altman Y, D'Angelo M, Salvesen GS, Drag M
Journal of the American Chemical Society 2017, 1
DOI: 10.1021/jacs.7b04394

Recent papers

Addition of thiols to the double bond of dipeptide C -terminal dehydroalanine as a source of new inhibitors of cathepsin C
Lenartowicz, P.; Makowski, M.; Oszywa, B.; Haremza, K.; Latajka, R.; Pawełczak, M.; Kafarski, P.
Biochimie 2017, 139, 46
DOI: 10.1016/j.biochi.2017.05.011

Abstract
Addition of thiols to double bond of glycyl-dehydroalanine and phenyl-dehydroalanine esters provided micromolar inhibitors of cathepsin C. The structure-activity studies indicated that dipeptides containing N-terminal phenylalanine exhibit higher affinity towards the enzyme. A series of C-terminal S-substituted cysteines are responsible for varying interaction with S1 binding pocket of cathepsin C. Depending on diastereomer these compounds most likely act as slowly reacting substrates or competitive inhibitors. This was proved by TLC analysis of the medium in which interaction of methyl (S)-phenylalanyl-(R,S)-(S-adamantyl)cysteinate (7i) with the enzyme was studied. Molecular modeling enabled to establish their mode of binding showed that S2 pocket is long and narrow and accommodates phenyl group of phenylalanine while significantly spacious sites located at the surface of the enzyme (one of them being S1 pocket) bind the adamantyl moiety oriented in different direction for each stereoisomer. Finally replacement of carboxymethyl moiety of methyl (S)-phenylalanyl-(R,S)-(S-phenyl)cysteinate (7c) with nitrile group provided about 650-times more potent inhibitor of cathepsin C indicating that the studied C-terminal S-substituted cysteines are good activity probes for S1 binding pocket of this enzyme.

Recent papers

Diethyl boronobenzylphosphonates as substrates in Suzuki–Miyaura reaction
Rydzewska, A.; Mangold, A,; Wanat, W.; Kafarski, P.
Phosphorus, Sulfur, Silicon Relat. Elements 2017, 192, 758
DOI: 10.1080/10426507.2017.1284845

Abstract
N-substituted boronobenzylphosphonates were evaluated as substrates in Suzuki–Miyaura couplingcatalyzed by tetrakis(triphenylphosphine)palladium(0) and complex of palladium acetate and (2-biphenyl)dicyclohexylphosphine. It was proven that they may be considered as useful substrates for thepreparation of functionalized aminophosphonates.

Recent papers

Michael additions to double bonds of esters of N-protected (s)-phenylalanyldehydroalanine (X-(s)-Phe-ΔAla-OMe) and its phosphonic acid counterpart (X-(s)-Phe-ΔAla-PO(OEt)2)
Lenartowicz, P., Dziuk, B.; Zarychta, B.; Makowski, M.; Kafarski P.
Phosphorus, Sulfur, Silicon Relat. Elements 2017, 192, 706
DOI: 10.1080/10426507.2017.1308933

Abstract
Electrophilic addition of amines, thiols and bromide to the double bonds of model dehydrodipeptides and dehydrophosphonodipeptide was studied. The double bond in these two classes of peptides reacted similarly and gave the same products. These results indicate that dehydropeptides are very good candidates assubstrates for modifications of peptide side-chain

Recent papers

Synthesis of fluorescent aminophosphonates by green chemistry proced
Kuśnierz, A.; Chmielewska E,
Phosphorus, Sulfur, Silicon Relat. Elements 2017, 192, 700
DOI: 10.1080/10426507.2017.130

Abstract
Fluorescent aminophosphonates were obtained using optimized conditions of the microwave-stimulatedKabachnik-Fields reaction. Unfortunately, in the case of more demanding, bulky amines and aldehydes thisreaction failed to give the desired products.

Recent papers

Glycosylation is important for legumain localization and processing to active forms but not for cystatin E/M inhibitory functions
Lunde NN, Haugen MH, Bodin Larsen KB, Damgaard I, Pettersen SJ, Kasem R, Rut W, Drag M, Poreba M, Johansen HT, Solberg R
Biochimie 2017, 139, 27
DOI: 10.1016/j.biochi.2017.05.009

Recent papers

Return of the Ice Age: Caspases Safeguard against Inflammatory Cell Death
Poreba M, Salvesen GS
Cell Chemical Biology 2017, 24, 550
DOI: 10.1016/j.chembiol.2017.05.001

Recent papers

The application of organophosphorus flame-retardants in epoxy resin
A. Bereska, P. Kafarski, B, Bereska, B. Tkacz, J. Iłowska, J. Lenza
J. Vinyl. Addit. Technol. 2017, 21, 142
DOI: 10.1002/vnl.21492

Abstract
The influence of two novel aryl phosphate mixtures on fire retardancy and the thermal stability of epoxy resin were studied. Combustion behavior, decomposition pathway, and thermal and thermo-oxidative degradation of the epoxy resin were examined by using the limiting oxygen index, vertical burning test (UL-94), cone calorimeter test, thermogravimetric analysis, and thermogravimetry coupled with Fourier-transform infrared spectroscopy. The morphology of the residues from the degradation of flame-retarded epoxy resins was investigated by using scanning electron microscopy. Data from the cone calorimeter test demonstrated that the total heat evolved, heat release rate, and peak heat release rate decreased significantly when the epoxy resin contained these retardants. Moreover, a 20 wt% of both phosphate mixtures in the epoxy resin allowed for a satisfactory oxygen index (30–33%) and for UL-94 V2 to be achieved. The condensed-phase and gas-phase actions of these aryl phosphate flame-retardants are proposed as the mode of flame-retardancy in epoxy resins.