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Wyszukujesz frazę "Poręba, Marcin" wg kryterium: Autor


Wyświetlanie 1-2 z 2
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 1-2 z 2

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