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Wyświetlanie 1-3 z 3
Tytuł:
Proteolityczny kombinat i jego regulatory
The proteolytic machinery and its regulators
Autorzy:
Stój, J.
Karpowicz, P.
Powiązania:
https://bibliotekanauki.pl/articles/171680.pdf
Data publikacji:
2012
Wydawca:
Polskie Towarzystwo Chemiczne
Tematy:
proteasom
system ubikwityno-proteasomalny
inhibitor
allosteryczność
proteasome
ubiquitin-proteasome system
allostery
Opis:
One of the proteolytic pathways existing in a cell is ubiquitin- proteasome system (UPS). This highly organized and ATP-dependent system is based on the multifunctional enzyme – the proteasome. Ubiquitin in this pathway plays a role of a tag which marks proteins intended for destruction. Ubiquitylated proteins are recognized and degraded by the 26S proteasome. It consists of a cylindrical-shaped proteolytic core – the proteasome 20S, and attached to it regulatory particles 19S (Fig. 2). The core is composed of four rings, each of them formed by seven subunits. The inner â-rings harbour active sites (in Eukaryota two of each kind: chymotrypsin-like (ChT-L), trypsin-like (T-L) and peptidylglutamyl (PGPH)). The outer, á-rings create a gated channel leading to the catalytic chamber [8]. In a latent proteasome the gate is closed by tightly packed N-terminal residues of á subunits (Fig. 4). Due to such architecture the active sites of the proteasome are not freely available for the substrates. An opening of the gate in physiological conditions occurs after binding the activators such as 11S, 19S or PA200. By catalysing degradation of proteins, the UPS is deeply involved in regulation of cellular physiology. It is also involved in removing of misfolded or damaged proteins and supports the immune system by generating antigenic peptides. Defects in functioning of this proteolytic system play a causal role in the development of a number of diseases, including inflammation, neurodegenerative diseases and various cancers [2–6] what is the reason why the proteasome has become an important therapeutic target. Detailed information about the structure, catalytic activities and mechanisms of functioning of the different proteasome complexes existing in cells is essential to understand their role in organisms as well as to develop new compounds which may find pharmaceutical application.
Źródło:
Wiadomości Chemiczne; 2012, 66, 11-12; 1097-1118
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
Tytuł:
Aminokwasy, glikany, peptydy i białka w ścieżkach diagnostycznych i terapeutycznych chorób cywilizacyjnych XXI wieku : projektowanie i charakterystyka fizykochemiczna oraz strukturalna
Amino acids, glycans, peptides and proteins in the diagnostic and therapeutic pathways of the 21st century civilization diseases : design, physicochemical and structural characterisation
Autorzy:
Bylińska, Irena
Dzierżyńska, Maria
Giżyńska, Małgorzata
Guzow, Katarzyna
Jankowska, Elżbieta
Jurczak, Przemysław
Kaczyński, Zbigniew
Karska, Natalia
Kowalczyk, Agnieszka
Kuncewicz, Katarzyna
Orlikowska, Marta
Sawicka, Justyna
Spodzieja, Marta
Szpakowska, Nikola
Szymańska, Aneta
Wieczerzak, Ewa
Witkowska, Julia
Rodziewicz-Motowidło, Sylwia
Powiązania:
https://bibliotekanauki.pl/articles/2200549.pdf
Data publikacji:
2022
Wydawca:
Polskie Towarzystwo Chemiczne
Tematy:
fluorophores
fluorescence spectroscopy
antimicrobial activity
anticancer activity
Cystapep
Stahylococcus aureus
antimicrobial compounds
amyloidogenic protein
mutagenesis
fibrilization
proteasome
aging
neurodegeneration
self-assembling peptides
tissue engineering
biomaterials
immune checkpoints
peptide inhibitors
immunotherapy
ligands of TAP protein
viral diseases
NMR structure of the UL49.5 protein
glycans
glycoconjugates
fluorofory
spektroskopia fluorescencyjna
aktywność przeciwdrobnoustrojowa
aktywność antynowotworowa
Staphylococcus aureus
związki przeciwbakteryjne
białko amyloidogenne
mutageneza
fibrylizacja
proteasom
procesy starzeniowe
neurodegeneracja
peptydy samoorganizujące
inżynieria tkankowa
biomateriały
punkty kontrolne układu immunologicznego
inhibitory peptydowe
immunoterapia
ligandy białka TAP
choroby wirusowe,
struktura NMR białka UL49.5
glikany
glikokoniugaty
Opis:
The civilization diseases of the 21st century are non-infectious disorders, affecting a large part of modern society. They are associated with the significant development of industry and technology, and hence with environmental pollution and an unhealthy lifestyle. These factors have led to the development of many civilization diseases, which currently include: cardiovascular diseases, respiratory diseases, diabetes, obesity, malignant tumors, gastrointestinal diseases, mental disorders and allergic diseases. The development of technologies, including modern therapies and new drugs, resulted in increase in life expectancy. This creates a global problem of an aging population with an increasing number of diseases of the old age, i.e. dementias. In addition, sedentary lifestyles and changing diets are the reasons why more and more people develop metabolic diseases, as well as neurological and cognitive disorders characterized by progressive damage to nerve cells and dementia. Currently, problem on a global scale is also the growing resistance to existing antimicrobial drugs. Therefore, the scientists face many challenges related to searching for the causes of these diseases, their diagnosis and treatment. Scientific research conducted at the Department of Biomedical Chemistry at the Faculty of Chemistry of the University of Gdańsk is part of this research trend. In this publication, we discuss various research topics with the long-term aim of solving the problems associated with the diseases mentioned above. The following chapters are dedicated to (i) looking for new effective fluorophores with diagnostic and anti-cancer activity; (ii) designing of new compounds with antibacterial and antiviral activity and their synthesis; (iii) investigating the mechanisms of amyloid deposit formation by human cystatin C and possibilities of inhibition of this process; (iv) designing and studies of compounds activating the proteasome with the potential to suppress the development of neurodegenerative diseases; (v) designing peptide fibrils and hydrogels as drug carriers; (vi) searching for peptide inhibitors of immune checkpoint as potential drugs for immunotherapy; (vii) studying the mechanism of action of selected herpesviruses by determining the structure of viral proteins and (viii) studying the composition of natural glycans and glycoconjugates in order to better understand the mechanisms of interaction of bacteria with the environment or with the host.
Źródło:
Wiadomości Chemiczne; 2022, 76, 5-6; 393--431
0043-5104
2300-0295
Pojawia się w:
Wiadomości Chemiczne
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

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