A5048034517- Peptidase Inhibition and Analysis
- Pneumocystis jirovecii pneumonia detection and treatment
- Protease and Inhibitor Mechanisms
- Chemical Synthesis and Analysis
- Bone Metabolism and Diseases
- Carbohydrate Chemistry and Synthesis
- Natural product bioactivities and synthesis
- Oral and gingival health research
- Neuropeptides and Animal Physiology
- Protein Hydrolysis and Bioactive Peptides
- Studies on Chitinases and Chitosanases
- Phytase and its Applications
- Organophosphorus compounds synthesis
- Fungal Plant Pathogen Control
- Enzyme Catalysis and Immobilization
- Antimicrobial Peptides and Activities
- Agriculture, Plant Science, Crop Management
- Cell Adhesion Molecules Research
- Venomous Animal Envenomation and Studies
- Microbial Metabolic Engineering and Bioproduction
- Microbial Metabolites in Food Biotechnology
- Ferrocene Chemistry and Applications
- Cellular transport and secretion
- Garlic and Onion Studies
- Bioeconomy and Sustainability Development
University of Opole
2014-2023
Wrocław University of Science and Technology
2005
Seven crystal structures of alanyl aminopeptidase from Neisseria meningitides (the etiological agent meningitis, NmAPN) complexed with organophosphorus compounds were resolved to determine the optimal inhibitor-enzyme interactions. The enantiomeric phosphonic acid analogs Leu and hPhe, which correspond P1 amino residues well-processed substrates, used assess impact absolute configuration stereospecific hydrogen bond network formed between aminophosphonate polar head active site on binding...
Mammalian cathepsin C is primarily responsible for the removal of N-terminal dipeptides and activation several serine proteases in inflammatory or immune cells, while its malarial parasite ortholog dipeptidyl aminopeptidase 1 plays a crucial role catabolizing hemoglobin host erythrocyte. In this report, we describe systematic substrate specificity analysis three orthologs from Homo sapiens (human), Bos taurus (bovine) Plasmodium falciparum (malaria parasite). Here, present new approach with...
Abstract Synthesis, structural and biological studies of pentapeptides containing two ΔPhe residues ( Z E isomers) in position 2 4 peptide chain were performed. All the investigated peptides adopted bent conformation majority them could exist as different conformers solution. Only pentapeptides, free N ‐termini appeared to act weak inhibitors cathepsin C with slow‐binding, competitive mechanism inhibition, acids being bound slightly better than their methyl esters. Results molecular modeling...
Tetrapeptide p-nitroanilides containing (E)-dehydrophenylalanine were synthesized and evaluated as inhibitors substrates of cathepsin C. Peptides a free, unblocked amino group appeared to be quite good the enzyme, whereas fully protected peptides acted very weak inhibitors. Structural studies by means NMR CD, alongside with molecular modelling, have proved that these are hydrolysed in one step direct removal p-nitroaniline from tetrapeptide.
The stereoselective synthesis of 1-amino-2-alkylalkanephosphonic acids, namely, compounds bearing two chiral centers, was achieved by the condensation hypophosphorous acid salts (R)(+) or (S)(−)-N-α-methylbenzylamine with appropriate aldehydes in isopropanol. Simultaneous deprotection and oxidation action bromine water provided equimolar mixtures RS:RR SR:SS diastereomers desired acids. They appeared to act as moderate inhibitors kidney leucine aminopeptidase potency dependent on absolute...
The procedures for the synthesis of esters dehydropeptides containing C-terminal (Z)-dehydrophenylalanine and dehydroalanine have been elaborated. These appeared to be moderate or weak inhibitors cathepsin C, with some them exhibiting slow-binding behavior. As shown by molecular modeling, they are rather bound at surface enzyme not submersed in its binding cavities.
Ligands containing bulky aliphatic P1 residues exhibit a high affinity towards cytosolic leucine aminopeptidase, bizinc protease of biomedical significance. According to this specificity, series phosphonic and phosphinic compounds have been put forward as novel putative inhibitors the enzyme. These were derivatives methionine norleucine both single amino acids dipeptides. The designed synthesised tested peptidase isolated from porcine kidneys using an improved separation procedure affording...
In this paper, we present the solvolysis reaction of dipeptide analogues fluorinated aminophosphonates with simultaneous quantitative deprotection amino group. To best our knowledge, work is first reported example application in cathepsin C inhibition studies. The new molecules show moderate enzyme, which opens door to consider them as potential therapeutic agents. Overall, findings provide a avenue for development aminophosphonate-based inhibitors.
Inhibitory activity of 14 phosphonic analogues phenylglycine, substituted in aromatic ring by fluorine and chlorine, was determined towards porcine aminopeptidase N. The obtained data served as a basis for studying their interaction with the enzyme modelled use Schrödinger Release 2018 program. observed linearity between Gibbs free energy differences inhibitory constants indicated usefulness this binding mode compared bovine lens leucine aminopeptidase. Although both enzymes differ...
The inhibitory activity of 14 racemic phosphonic acid analogs phenylglycine, substituted in aromatic rings, towards porcine aminopeptidase N (pAPN) and barley seed was determined experimentally. obtained patterns the against two enzymes were similar. data served as a basis for studying binding modes these inhibitors by pAPN using molecular modeling. It found that their aminophosphonate fragments bound highly uniform manner difference affinities most likely resulted from mode substitution...
Abstract Three dehydrotetrapeptides of rationally varying structure were prepared and tested as affectors cathepsin C. These compounds appeared to be substrates the enzyme, being equipotent with their classical counterparts. Thus, replacement amino acid in a short peptide by corresponding dehydroamino does not prevent C recognizing dehydropeptide its substrate. Copyright © 2001 European Peptide Society John Wiley & Sons, Ltd.
Inhibitory potencies of 24 α-aminophosphonic acids against barley seeds (Hordeum vulgare L.) metallo-aminopeptidase have been determined to evaluate structural requirements this enzyme. The enzyme was sensitive mostly the influence phosphonic acid analogues phenylalanine and its homologues, thus showing narrow specificity if compared with porcine aminopeptidases M1 M17 Plasmodium aminopeptidase M17.
Abstract The selection of bioremediation techniques is important for purification contaminated soil agricultural use. Studies on with petroleum substances have indicated that the applied method remediation has a bigger impact development oat seedlings than level contamination. A yeast inoculum appeared to be technique which was friendliest vegetation