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    Wyświetlanie 1-4 z 4
    Tytuł:
    Monitorowanie aktywności proteolitycznej jako element diagnostyki chorób cywilizacyjnych
    Proteolityc activity monitoring as an element of diagnostics of civilization diseases
    Autorzy:
    Gruba, Natalia
    Romanowska, Anita
    Rejmak, Wiktoria
    Sikora, Honorata
    Wysocka, Magdalena
    Lesner, Adam
    Powiązania:
    https://bibliotekanauki.pl/articles/2200584.pdf
    Data publikacji:
    2022
    Wydawca:
    Polskie Towarzystwo Chemiczne
    Tematy:
    proteolytic enzymes
    substrate specificity
    civilization diseases
    cancerous diseases
    enzymy proteolityczne
    specyficzność substratowa
    choroba cywilizacyjna
    choroba nowotworowa
    Opis:
    Proteolytic enzymes are essential for the proper functioning of every living cell. Due to their great importance in controlling metabolic changes in living organisms, they could be used in the diagnosis of civilization diseases. Hence, the search for new methods of determining and controlling their activity is extremely important. Our team, has been studying substrates of proteases and their potential use in detection of biomarkers activity for many years.
    Źródło:
    Wiadomości Chemiczne; 2022, 76, 5-6; 335--347
    0043-5104
    2300-0295
    Pojawia się w:
    Wiadomości Chemiczne
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Narzędzia chemiczne do badania enzymów proteolitycznych przy użyciu cytometrii masowej
    Mass cytometry-compatible chemical probes for the investigation of proteolytic enzymes
    Autorzy:
    Groborz, Katarzyna
    Powiązania:
    https://bibliotekanauki.pl/articles/2200437.pdf
    Data publikacji:
    2022
    Wydawca:
    Polskie Towarzystwo Chemiczne
    Tematy:
    markery chemiczne
    cytometria masowa
    enzymy proteolityczne
    nowotwór
    śmierć komórki
    activity-based probes
    mass cytometry
    proteolytic enzymes
    cancer
    cell death
    Opis:
    Mass cytometry is one of the newest and most high-throughput technologies that allows for the investigation of complex biological systems at single cell level. It relies on the use of stable metal isotopes as labels of specific cell markers and therefore, allows for simultaneous analysis of more than 40 parameters at single cell level. In order to fully explore the potential of mass cytometry, researchers are trying to develop new experimental setups based on the application of pure metal isotopes in biological studies. The incorporation of antibodies into mass cytometry setups, while extremely selective and well-validated, limits the analysis as it shows the whole protein pool present in the cell. In our group, we developed new technology that allows for the identification of active forms of proteins-the ones that actively participate in cell signaling pathways. Activity-based probes are the most valuable tools for enzyme activity profiling and for years now they have been in the center of the method called Activity-Based Protein Profiling. Classic activity-based probes consist of three parts: a warhead (electrophilic binding group that covalently modifies enzyme active site), linker (specific peptide sequence or non-specific carbon chain) and the fluorescent tag that allows for enzyme detection and localization inside the cell. Spectral properties of commercially available fluorophores allow for the detection of up to dozen different cell parameters, with the use of various techniques such as confocal microscopy or flow cytometry. To increase the number of analyzed parameters, we designed activity-based probes that possess DOTA chelating moiety that is able to trap one metal atom per one probe. The combination of mass cytometry with highly selective activity-based probes allowed for the development of new technology that grants the possibility of multiparametric analysis of complex biological samples such as blood or cancer tissue. The new type of activity-based probes (so-called TOF-probes) incorporate various inhibitor scaffolds designed with HyCoSuL technology (Hybrid Combinatorial Substrate Libraries). These compounds possess a variety of unnatural amino acids in their structures, which significantly increases their selectivity toward proteases of interest.
    Źródło:
    Wiadomości Chemiczne; 2022, 76, 11-12; 864-880
    0043-5104
    2300-0295
    Pojawia się w:
    Wiadomości Chemiczne
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Visualization of proteolytic enzymes using mass cytometry : compatible chemical probes
    Wizualizacja enzymów proteolitycznych za pomocą sond chemicznych oraz cytometrii masowej
    Autorzy:
    Groborz, Katarzyna
    Poręba, Marcin
    Powiązania:
    https://bibliotekanauki.pl/articles/2057909.pdf
    Data publikacji:
    2021
    Wydawca:
    Polskie Towarzystwo Chemiczne
    Tematy:
    sonda chemiczna
    cytometria masowa
    enzymy proteolityczne
    nowotwory
    śmierć komórki
    chemical probe
    mass cytometry
    proteolytic enzymes
    cancer
    cell death
    Opis:
    Proteolytic enzymes, also known as peptidases or proteases, are protein catalysts that are primarily responsible for the hydrolysis of a peptide (amide) bond in peptide and protein substrates. By selective hydrolysis of selected substrates, these enzymes control many physiologically important processes including programmed cell death, blood coagulation cascade, protein maturation, fibrinolysis and many others. On the other hand, however, the imbalance in proteases activity leads to the development of diseases, including cancer, neurodegenerative diseases and coronary diseases etc.. In recent decades there has been great progress in studying the biological functions of many proteolytic enzymes. These observations were made possible through the use of various research techniques including genomics, epigenomics and proteomics. However, a major limitation of these techniques is the lack of information about the exact catalytic activity of the enzymes. For this reason, chemical probes are the most convenient toll for functional investigation of proteolytic enzymes. According to the generally accepted convention, chemical probes are compounds that can detect the catalytic activity of proteolytic enzymes. In general, chemical-based probes (activity-based probes, ABPs) consist of three main components: (1) a reactive binding group that binds permanently to the enzyme active site, (2) a recognition sequence (usually a peptide), which is responsible for the selective binding of a given probe to an individual enzyme or group of enzymes, and (3) a tag, mainly a fluorophore, enabling for detection of the probe-enzyme complex. However, the current limitation of ABPs is that only up to four enzymes can be detected and visualized in parallel, which significantly impedes their application for multi-parametric analysis. To date, the detection of proteases with the use of ABPs was limited to individual enzymes being investigated one by one, thus the obtained picture was far from being complete. In this review we describe the development of a new type of enzyme ABPs, so called TOF-probes that are compatible with mass cytometry format. The application of metal isotopes instead of fluorophores, makes possible to significantly increase the number of enzymes, which can be simultaneously visualized using chemical probes. Mass cytometry is a revolutionary technology that adopts atomic mass spectrometry into flow cytometry applications. The excellence of this method is that each metal isotope (mostly from lanthanides) has its own peak on mass spectrum, which eliminates the problem of signal overlap, thus allows for monitoring of more than 40 parameters at single cell level.
    Źródło:
    Wiadomości Chemiczne; 2021, 75, 11-12; 1171--1191
    0043-5104
    2300-0295
    Pojawia się w:
    Wiadomości Chemiczne
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Nienaturalne aminokwasy jako strategia do otrzymywania substratów, inhibitorów i niskocząsteczkowych sond aktywności dla enzymów proteolitycznych
    Unnatural amino acids as achemical tool for the development of protease substrates, inhibitors and activity - baseproblems
    Autorzy:
    Poręba, Marcin
    Kasperkiewicz-Wasilewska, Paulina
    Rut, Wioletta
    Drąg, Marcin
    Powiązania:
    https://bibliotekanauki.pl/articles/2200587.pdf
    Data publikacji:
    2022
    Wydawca:
    Polskie Towarzystwo Chemiczne
    Tematy:
    proteolytic enzymes
    substrate specificity
    unnatural amino acids
    substrates
    inhibitors
    activity-based probes
    caspases
    cathepsins
    neuthrophil serine proteases
    proteasome
    SARS-CoV-2 proteases
    enzymy proteolityczne
    specyficzność substratowa
    nienaturalne aminokwasy
    niskocząsteczkowe sondy aktywności
    kaspazy
    katepsyny
    proteasom
    proteazy wirusa SARS-CoV-2
    Opis:
    Proteolytic enzymes are molecular scissors that are responsible for the amide bond breakdown in peptide and protein substrates. Over the years, the view on proteases has been considerably changed from non-specific digestive enzymes to sophisticated biocatalysts, which by performing limited proteolysis control virtually all biological processes. In order to better understand how proteases work and what are their biologically relevant target substrates, it is indispensable to determine their catalytic preferences. This knowledge can be further utilized to develop selective substrates, inhibitors and activity-based probes (ABPs) enabling the monitoring of proteases activity in various settings, from in vitro analysis on recombinant enzymes or cell lysates to ex vivo and in vivo imaging at the single cell level. Among many chemical-based approaches that have been developed and applied over the years, the Hybrid Combinatorial Substrate Library (HyCoSuL) technology has emerged as one of the most powerful one. HyCoSuL is a combinatorial peptide-based library of fluorogenic substrates, that comprise natural and unnatural amino acids, that can deeply explore the chemical space in proteases active site, providing a structural framework for the development of highly-selective chemical tools. In this review we present the most prominent examples of proteolytic enzymes that have been profiled with HyCoSuL approach yielding selective substrates, potent inhibitors, and very sensitive activity-based probes.
    Źródło:
    Wiadomości Chemiczne; 2022, 76, 5-6; 433--454
    0043-5104
    2300-0295
    Pojawia się w:
    Wiadomości Chemiczne
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-4 z 4

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