Publications Artur Mucha

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Artur Mucha


Vassiliou, S.; Pagoni, A.; Węglarz-Tomczak, E.; Talma, M.; Tabor, W.; Grabowiecka, A.; Berlicki, Ł.; Mucha, A., Phosphinic acid-based enzyme inhibitors Phos. Sulph. Rel. El. 2022, 197, 451.


Pagoni, A.; Grabowiecka, A.; Tabor, W.; Mucha, A.; Vassiliou, S.; Berlicki, Ł., Covalent Inhibition of Bacterial Urease by Bifunctional Catechol-Based Phosphonates and Phosphinates J. Med. Chem. 2021, 64, 404.


Mucha, A.; Kafarski, P., Peptide and Pseudopeptide Bond Synthesis in Phosphorus Dipeptide Analogs. Methods Mol. Biol. 2020, 2103, 287.

Talma, M.; Mucha, A., P1′ Residue-Oriented Virtual Screening for Potent and Selective Phosphinic (Dehydro) Dipeptide Inhibitors of Metallo-Aminopeptidases Biomolecules 2020, 10, 659.

Janiszewska, K.; Talma, M.; Oszywa, B.; Pawełczak, M.; Kafarski, P.; Mucha, A.,, N-Benzyl Residues as the P1' Substituents in Phosphorus-Containing Extended Transition State Analog Inhibitors of Metalloaminopeptidases Molecules 2020, 25, 4334.


Burda‐Grabowska, M.; Macegoniuk, K.; Flick, R.; Nocek, B. P.; Joachimiak, A.; Yakunin, A. F.; Mucha, A.; Berlicki, Ł., Bisphosphonic acids and related compounds as inhibitors of nucleotide‐ and polyphosphate‐processing enzymes: A PPK1 and PPK2 case study. Chem. Biol. Drug Des. 2019, 93, 1197.

Talma, M.; Maślanka, M.; Mucha, A., Recent developments in the synthesis and applications of phosphinic peptide analogs. Bioorg. Med. Chem. Lett. 2019, 29, 1031.

Maślanka, M.; Mucha, A., Recent Developments in Peptidyl Diaryl Phoshonates as Inhibitors and Activity-Based Probes for Serine Proteases Pharmaceuticals 2019, 12, 86.


Piasta, K.; Dziełak, A.; Mucha, A.; Gumienna-Kontecka, E., Non-symmetrical bis(aminoalkyl)phosphinates: new ligands with enhanced binding of Cu(II) ions. New J. Chem. 2018, 42, 7737.

Ewelina Węglarz-Tomczak, Michał Talma, Mirosław Giurg, Hans V. Westerhoff, Robert Janowski and Artur Mucha, Neutral metalloaminopeptidases APN and MetAP2 as newly discovered anticancer molecular targets of actinomycin D and its simple analogs Oncotarget 2018, 9, 29365.

Ntatsopoulos, V.; Macegoniuk, K.; Mucha, A.; Vassiliou, S.; Berlicki, Ł., Structural exploration of cinnamate-based phosphonic acids as inhibitors of bacterial ureases. Eur. J. Med. Chem. 2018, 159, 307.

Nocek, B. P.; Khusnutdinova, A. N.; Ruszkowski, M.; Flick, R.; Burda, M.; Batyrova, K.; Brown, G.; Mucha, A.; Joachimiak, A.; Berlicki, Ł.; Yakunin, A. F., Structural insights into substrate selectivity and activity of bacterial polyphosphate kinases ACS Catal. 2018, 8, 10746.


Rydzewska, A.; Olender, A.; Mucha, A.; Kafarski, P., Diethyl boronobenzylphosphonates as substrates in Petasis reactions ARKIVOC 2017, 2017, 107.

Talma, M.; Mucha, A., P-C bond formation in reactions of Morita-Baylis-Hillman adducts with phosphorus nucleophiles. Arkivoc 2017, 2017, 324.

Ntatsopoulos, V.; Vassiliou, S.; Macegoniuk, K.; Berlicki, Ł.; Mucha, A., Novel organophosphorus scaffolds of urease inhibitors obtained by substitution of Morita-Baylis-Hillman adducts with phosphorus nucleophiles Eur. J. Med. Chem. 2017, 133, 107.

Macegoniuk, K.; Grela, E.; Biernat, M.; Psurski, M.; Gościniak, G.; Dziełak, A.; Mucha, A.; Wietrzyk, J.; Berlicki, Ł.; Grabowiecka, A., Aminophosphinates against Helicobacter pylori ureolysis—Biochemical and whole-cell inhibition characteristics PLoS One 2017, 1, 182437.


Węglarz-Tomczak, E.; Berlicki, Ł.; Pawełczak, M.; Nocek, B.; Joachimiak, A. Mucha, A., A structural insight into the P1-S1 binding mode of diaminoethylphosphonic and phosphinic acids, selective inhibitors of alanine aminopeptidases. Eur. J. Med. Chem. 2016, 117, 187.

Węglarz-Tomczak, E.; Vassiliou, S.; Mucha, A., Discovery of potent and selective inhibitors of human aminopeptidases ERAP1 and ERAP2 by screening libraries of phosphorus-containing amino acid and dipeptide analogues. Bioorg. Med. Chem. Lett. 2016, 26, 4122.

Węglarz-Tomczak, E.; Staszewska, K.; Talma, M.; Mucha, A., Enantiomeric a,ß-diaminoethylphosphonic acids as potent inhibitors of aminopeptidases — stereoselective synthesis and biological activity. Tetrahedron Lett. 2016, 57, 4812.

Węglarz-Tomczak, E.; Burda-Grabowska, M.; Giurg, M.; Mucha, A., Identification of methionine aminopeptidase 2 as a molecular target of the organoselenium drug ebselen and its derivatives/analogues: Synthesis, inhibitory activity and molecular modeling study. Bioorg. Med. Chem. Lett. 2016, 26, 5254.

Grela, E.; Dziełak, A.; Szydowska, K.; Mucha, A.; Kafarski, P.; Grabowiecka, A.M., Whole-cell Proteus mirabilis urease inhibition by aminophosphinates for the control of struvite formation. J. Med. Microbiol. 2016, 65, 1123.


Macegoniuk, K.; Dziełak, A.; Mucha, A.; Berlicki, Ł., Bis(aminomethyl)phosphinic acid, a highly promising scaffold for the development of bacterial urease inhibitors. ACS Med. Chem. Lett. 2015, 6, 146.

Dziełak, A.; Mucha, A., Catalytic and MW-Assisted Michaelis-Arbuzov Reactions Curr. Green Chem. 2015, 2, 223.

Rudzińska-Szostak, E.; Górecki, Ł. Berlicki, Ł.; Ślepokura, K.; Mucha, A., Zwitterionic Phosphorylated Quinines as Chiral Solvating Agents for NMR Spectroscopy Chirality 2015, 27, 752.


Klimek-Ochab, M.; Mucha, A.; Żymań„czyk-Duda, E, 2-Aminoethylphosphonate Utilization by the Cold-Adapted Geomyces pannorum P11 Strain Curr. Microbiol. 2014, 68, 330.

Górecki, Ł.; Mucha, A.; Kafarski, P., Addition of H-phosphonates to quinine-derived carbonyl compounds. An unexpected C9 phosphonate–phosphate rearrangement and tandem intramolecular piperidine elimination. Beilstein J. Org. Chem. 2014, 10, 883.

Vassiliou, S.; Węglarz-Tomczak, E.; Berlicki, Ł.; Pawełczak, M.; Nocek, B.; Mulligan, R.; Joachimiak, A.; Mucha, A., Structure-guided, single-point modifications in the phosphinic dipeptide structure yield highly potent and selective inhibitors of neutral aminopeptidases. J. Med. Chem. 2014, 57, 8140.


Węglarz-Tomczak, E.; Poręba, M.; Byzia, A.; Berlicki, Ł.; Nocek, B.; Mulligan, R.; Joachimiak, A.; Drąg, M.; Mucha, A., An integrated approach to the ligand binding specificity of Neisseria meningitidis M1 alanine aminopeptidase by fluorogenic substrate profiling, inhibitory studies and molecular modeling. Biochimie 2013, 95, 419.


Górecki, Ł.; Berlicki, Ł.; Mucha, A.; Kafarski, P.; Ślepokura, K.; Rudzińska-Szostak, E., Phosphorylation as a Method of Tuning the Enantiodiscrimination Potency of Quinine – an NMR Study. Chirality 2012, 24, 318.

Mucha, A., Synthesis and Modifications of Phosphinic Dipeptide Analogues Molecules 2012, 17, 13530.


Pícha, J.; Liboska, R.; Buděšínský, M.; Jiráček, J.; Pawełczak, M.; Mucha, A., Unusual activity pattern of leucine aminopeptidase inhibitors based on phosphorus containing derivatives of methionine and norleucine. J. Enz. Inhib. Med. Chem. 2011, 26, 155.

Dziełak, A.; Pawełczak, M.; Mucha, A. , A three-component Mannich-type condensation leading to phosphinic dipeptides – extended transition state analogue inhibitors of aminopeptidases. Tetrahedron Lett. 2011, 52, 3141.

Mucha, A.; Kafarski, P.; Berlicki, Ł., Remarkable potential of the alpha-aminophosphonate/phosphinate structural motif in medicinal chemistry. J. Med. Chem. 2011, 54, 5955.


Skinner-Adams, T. S.; Stack, C. M.; Trenholme, K. R.; Brown, C. L.; Grembecka, J.; Lowther, J.; Mucha, A.; Drag, M.; Kafarski, P.; McGowan, S.; Whisstock, J. C.; Gardiner, D. L.; Dalton, J. P., Plasmodium falciparum neutral aminopeptidases: new targets for anti-malarials. Trends Biochem. Sci. 2010, 35, 53.

McGowan, S.; Oellig, C. A.; Birru, W. A.; Caradoc-Davies, T. T.; Stack, C. M.; Lowther, J.; Skinner-Adams, T.; Mucha, A.; Kafarski, P.; Grembecka, J.; Trenholme, K. R.; Buckle, A. M.; Gardiner, D. L.; Dalton, J. P.; Whisstock, J. C. , Structure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases. Proc. Natl. Acad. Sci. U. S. A. 2010, 107, 2449.

Mucha, A.; Drą…g, M.; Dalton, J. P.; Kafarski, P., Metallo-aminopeptidase inhibitors. Biochimie 2010, 92, 1509.


McGowan, S.; Porter, C. J.; Lowther. J.; Stack, C. M.; Golding, S. J.; Skinner-Adams, T. S.; Trenholme, K. R.; Teuscher, F.; Donnelly, S. M.; Grembecka, J.; Mucha, A.; Kafarski, P.; Degori, R.; Buckle, A. M.; Gardiner, D. L.; Whisstock, J. C.; Dalton, J. P., Structural basis for the inhibition of the essential Plasmodium falciparum M1 neutral aminopeptidase. Proc. Natl. Acad. Sci. U. S. A. 2009, 106, 2537.

Dąbrowska, E.; Burzyńska, A.; Mucha, A.; Matczak-Jon, E.; Sawka-Dobrowolska, W.; Berlicki, Ł.; Kafarski, P., Insight into the mechanism of three component condensation leading to aminomethylenebisphosphonates. J. Organomet. Chem. 2009, 694, 3806.

Rudzińska, E.; Berlicki, Ł.; Kafarski, P.; Lammerhofer, M.; Mucha, A., Cinchona alkaloids as privileged chiral solvating agents for enantiodiscrimination of N-protected aminoalkanephosphonates - a comparative NMR study. Tetrahedron Asymmetry 2009, 20, 2709.


Mucha, A.; Laemmerhofer, M.; Lindner, W.; Pawełczak, M.; Kafarski, P., Individual stereoisomers of phosphinic dipeptide inhibitor of leucine aminopeptidase. Bioorg. Med. Chem. Lett. 2008, 18, 1550.

Latajka, R.; Krężel, A.; Mucha, A.; Jewgiński, M.; Kafarski, P., Conformational investigations of bis(alpha-aminoalkyl)phosphinic acids and studies of the stability of their complexes with Cu(II). J. Mol. Str. 2008, 877, 64.


Rudzińska, E.; Poliwoda, A.; Berlicki, Ł.; Mucha, A.; Dżygiel, P.; Wieczorek, P.P.; Kafarski, P., Enantiodifferentiation of N-benzyloxycarbonylaminophosphonic and phosphinic acids and their esters using cyclodextrins by means of capillary electrophoresis. J. Chromat. A 2007, 1138, 284.

Stack, C. M.; Lowther, J.; Cunningham, E.; Donnelly, S.; Gardiner, D. L.; Trenholme, K. R.; Skinner-Adams, T. S.; Teuscher, F.; Grembecka, J.; Mucha, A.; Kafarski, P.; Lua, L.; Bell, A.; Dalton, J. P., Characterization of the Plasmodium falciparum M17 leucyl aminopeptidase. A protease involved in amino acid regulation with potential for antimalarial drug development. J. Biol. Chem. 2007, 282, 2069.

Rudzińska, E.; Berlicki, Ł.; Mucha, A.; Kafarski, P., Analysis of pD Dependent Complexation of N-Benzyloxycarbonylaminophosphonic Acids by a-Cyclodextrin. Enantiodifferentation of Phosphonic Acid pKa V alues Chirality 2007, 19, 764.

Rudzińska, E.; Berlicki, Ł.; Mucha, A.; Kafarski, P., Chiral discrimination of ethyl and phenyl N-benzyloxycarbonylaminophosphonates by cyclodextrins. Tetrahedron Asymmetry 2007, 18, 1579.

Berlicki, Ł.; Mucha, A.; Kafarski, P., A mild and convenient oxidation of H-phosphinic acids. Pol. J. Chem. 2007, 81, 1959.

Vassiliou, S.; Xeilari, M.; Yiotakis, A.; Grembecka, J.; Pawelczak, M.; Kafarski, P.; Mucha, A., A synthetic method for diversification of the P1 ' substituent in phosphinic dipeptides as a tool for exploration of the specificity of the S1 ' binding pockets of leucine aminopeptidases. Bioorg. Med. Chem. 2007, 15, 3187.

Teuscher, F.; Lowther, J.; Skinner-Adams, T.S.; Spielmann, T.; Dixon, M.W.A.; Stack, C.M.; Donnelly, S.; Mucha, A.; Kafarski, P.; Vassiliou, S.; Gardiner, D.L.; Dalton, J.P.; Trenholme, K.R., The M18 Aspartyl Aminopeptidase of the Human Malaria Parasite Plasmodium falciparum. J. Biol. Chem. 2007, 282, 30817.

Skinner-Adams, T. S.; Lowther, J.; Teuscher, F.; Stack, C. M.; Grembecka, J.; Mucha, A.; Kafarski, P.; Trenholme, K. R.; Dalton, J. P.; Gardiner, D. L., Identification of Phosphinate Dipeptide Analog Inhibitors Directed against the Plasmodium falciparum M17 Leucine Aminopeptidase as Lead Antimalarial Compounds. J. Med. Chem. 2007, 50, 6024.


Biał‚as, A.; Grembecka, J.; Krowarsch, D.; Otlewski, J.; Potempa, J.; Mucha, A., Exploring the Sn Binding Pockets in Gingipains by Newly Developed Inhibitors: Structure-Based Design, Chemistry and Activity. J. Med. Chem. 2006, 49, 1744.

Mucha, A.; Kunert, A.; Grembecka, J.; Pawelczak, M.; Kafarski, P., A phosphonamidate containing aromatic N-terminal amino group as inhibitor of leucine aminopeptidase-design, synthesis and stability. Eur. J. Med. Chem. 2006, 41, 768.

Preinerstorfer, B.; Lubda, D.; Mucha, A.; Kafarski, P.; Lindner, W.; Lämmerhofer, M., Stereoselective separations of chiral phosphinic acid pseudodipeptides by CEC using silica monoliths modified with an anion-exchange-type chiral selector. Electrophoresis 2006, 27, 4312.

Mucha, A., Fosfonamidowe oraz fosfinopeptydowe inhibitory metaloproteaz. Monografie Wydziału Chemicznego Politechniki Wrocławskiej 2006, 1, 1.


Gał‚ezowska, J.; Sobek, S.; Drag, M.; Mucha, A.; Kafarski, P.; Kozł‚owski, H. , Specific interactions of divalent metal ions with phosphonic analogues of dipeptide inhibitors of proteases. Pol. J. Chem. 2005, 79, 603.

Firczuk, M.; Mucha, A.; Bochtler, M. , Crystal structures of active LytM. J. Mol. Biol. 2005, 354, 579.


Berlicki, Ł.; Rudzińska, E.; Mucha, A.; Kafarski, P., Cyclodextrins as NMR probes in the study of the enantiomeric compositions of N-benzyloxycarbonylamino-phosphonic and phosphinic acids. Tetrahedron-Asymmetry 2004, 15, 1597.

Mucha, A.; Pawelczak, M.; Hurek, J.; Kafarski, P., Synthesis and activity of phosphinic tripeptide inhibitors of cathepsin C. Bioorg. Med. Chem. Lett. 2004, 14, 3113.


Kafarski, P.; Grembecka, J.; Mucha, A.; Pawełczak, M.; Drąg, M.; Berlicki, Ł.; Olechnowicz, D., Projektowanie Potencjalnych Leków i Pestycydów z Wykorzystaniem Wiedzy o Strukturze Przestrzennej Enzymów. Przem. Chem. 2003, 82, 1087.

Mucha, A.; Grembecka, J.; Cierpicki, T.; Kafarski, P., Hydrolysis of the phosphonamidate bond in phosphono dipeptide analogues - The influence of the nature of the N-terminal functional group. Eur. J. Org. Chem. 2003, 4797.

Grembecka, J.; Mucha, A.; Cierpicki, T.; Kafarski, P., The most potent organophosphorus inhibitors of leucine aminopeptidase. Structure-based design, chemistry, and activity. J. Med. Chem. 2003, 46, 2641.

Lammerhofer, M.; Hebenstreit, D.; Gavioli, E.; Lindner, W.; Mucha, A.; Kafarski, P.; Wieczorek, P., High-performance liquid chromatographic enantiomer separation and determination of absolute configurations of phosphinic acid analogues of dipeptides and their alpha-aminophosphinic acid precursors. Tetrahedron-Asymmetry 2003, 14, 2557.


Grembecka, J.; Mucha, A.; Cierpicki, T.; Kafarski, P., Structure-based design and synthesis of dipeptide analogues as new inhibitors of leucine aminopeptidase. Phosphorus, Sulfur 2002, 177, 1739.

Mucha, A.; Grembecka, J.; Białas, A.; Stachowiak, D.; Otlewski, J.; Potempa,J., Design, Synthesis and Activity of Chloromethyl Ketone Inhibitors of Gingipains. Proceeding of the 27th European Peptide Symposium 2002, 988.

Mucha, A.; Kafarski, P., Transesterification of Monophenyl Phosphonamidates - Chemical Modelling of Serine Protease Inhibition. Tetrahedron 2002, 58, 5855.


Mucha, A.; Grembecka, J.; Cierpicki, T.; Kafarski P., The Synthesis of Phosphonamidate and Phosphinic Dipeptide Analogues - Inhibitors of Leucine Aminopeptidase. Biologically Active Peptides. VIIth Conference. Collection Symposium Series 2001, 4, 28.


Vassiliou, S.; Mucha, A.; Cuniasse, P.; Georgiadis, D.; Lucet-Levannier, K.; Beau, F.; Kannan, R.; Murphy, G.; Knauper, V.; Rio, M.-C.; Basset, P.; Yiotakis, A.; Dive, V., Phosphinic Pseudo-Tripeptides as Potent Inhibitors of Matrix Metalloproteinases: A Structure - Activity Study. J. Med. Chem. 1999, 42, 2610.

Holtz, B.; Cuniasse, P.; Boulay, A.; Kannan, R.; Mucha, A.; Beau, F.; Basset, P.; Dive, V., Role of the S1' Subsite Glutamine 215 in Activity and Specificity of Stromelysin-3 by Site-Directed Mutagenesis. Biochemistry 1999, 38, 12174.

Stano, A.; Mucha, A.; Kafarski, P., Reaction of N-(Benzyloxycarbonyl)amino-benzylphosphonous Acid with Triethyl Orthoformate. Synth. Commun. 1999, 29, 4269.


Mucha, A.; Cuniasse, P.; Kannan, R.; Beau, F.; Yiotakis, A.; Basset, P.; Dive, V., Membrane Type-1 Matrix Metalloprotease and Stromelysin-3 Cleave More Efficiently Synthetic Substrates Containing Unusual Amino Acids in Their P1 Positions. J. Biol. Chem. 1998, 273, 2763.


Mucha, A.; Kafarski, P.; Plenat, F.; Cristau, H.-J., Preparation of Benzyl N-Benzyloxycarbonylaminophosphonates and -Aminophospinates - the Scope and Limitations of O-Benzyl-N,N'-dicyclohexylisourea Method. Phosphorus, Sulfur and Silicon 1995, 105, 187.

Mucha, A.; Tyka, R.; Kafarski, P.; Głowiak, T.; Goplańska, A., Preparation, Crystal and Molecular Structure and Evaluation of Plant Growth Regulating Activity of Guanidinoalkanephosphinates and Phosphonates. Heteroatom Chem. 1995, 6, 433.


Mucha, A.; Kafarski, P.; Plenat, F.; Cristau, H.-J., The Preparation of Phosphono Peptides Containing a Phosphonamidate Bond. Tetrahedron 1994, 50, 12743.

Mucha, A.; Tyka, R.; Sawka-Dobrowolska, W.; Głowiak, T., Resolution, Crystal Structure and Absolute Configuration of the Enantiomers of Aminophenylmethane-phosphonous Acid Hydrate. Phosphorus, Sulfur and Silicon 1994, 92, 129.