Informacja

Drogi użytkowniku, aplikacja do prawidłowego działania wymaga obsługi JavaScript. Proszę włącz obsługę JavaScript w Twojej przeglądarce.

Wyszukujesz frazę "amyloid-β" wg kryterium: Temat


Wyświetlanie 1-2 z 2
Tytuł:
Rola metali w rozwoju choroby Alzheimera i Parkinsona
The role of metals in development Alzheimer's and Parkinson's diseases
Autorzy:
Żygowska, Justyna
Szymańska, Aneta
Powiązania:
https://bibliotekanauki.pl/articles/2057913.pdf
Data publikacji:
2022
Wydawca:
Polskie Towarzystwo Chemiczne
Tematy:
choroba neurodegeneracyjna
jony metali
β-amyloid
białka amyloidogenne
choroba Alzheimera
choroba Parkinsona
neurodegenerative diseases
amyloidogenic proteins
amyloid β
metal ions
Alzheimer's disease
Parkinson disease
Opis:
Neurodegenerative diseases are the consequence of progressive brain degeneration caused by the death of nerve cells. Many factors that influence the neurodegeneration development are still not fully known. A lot of studies indicate the contribution of metal ions in this process. Copper, zinc, and iron are trace elements essential for proper functioning of the body. They are part of many enzymes participating in the transmission of the nerve signals, electrons transport, neurotransmitters and nucleic acids synthesis, and oxygen storage. Disorder of metals homeostasis leads to the development of severe diseases and nervous system degenerations. An excess of copper and iron ions causes a significant increase in cellular oxidative stress. Metals catalyze the reactions of free radicals formation that destroy proteins, lipids, and nucleic acids. High concentration of copper and iron ions were found in the deposits of amyloidogenic proteins. Amyloid β (Alzheimer disease) and α synuclein (Parkinson disease) have ions binding chain structures. The metal-protein interaction increases oligomerization speed in vitro. A lot of evidence suggests that the disorder of Cu, Zn and Fe homeostasis accelerates the progress of brain neurodegeneration. Human organism contains many metals, which are not needed for the proper functioning of the body, e.g. aluminum. Al binds to nucleic acids causing an increase in cellular oxidative stress and initiating proteins oligomerization. The presence of aluminum is also considered to be disadvantageous for the nervous system. The lack of medicines for neurodegenerative diseases forces us to search for new therapies. The development of degenerations could be slowed down by chelators of toxic metals, but first, these diseases must be better understood. Adverse effects of high concentration of metal ions on brain functioning are not fully known. This knowledge is necessary to find effective drugs.
Źródło:
Wiadomości Chemiczne; 2022, 76, 1-2; 1-25
0043-5104
2300-0295
Pojawia się w:
Wiadomości Chemiczne
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Circular dichroism and aggregation studies of amyloid β (11-8) fragment and its variants.
Autorzy:
Juszczyk, Paulina
Kołodziejczyk, Aleksandra
Grzonka, Zbigniew
Powiązania:
https://bibliotekanauki.pl/articles/1041423.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
secondary structure studies
thioflavine T assay
aggregation studies.
Alzheimer's disease
amyloid β
circular dichroism (CD)
Opis:
Aggregation of Aβ peptides is a seminal event in Alzheimer's disease. Detailed understanding of Aβ assembly would facilitate the targeting and design of fibrillogenesis inhibitors. Here comparative conformational and aggregation studies using CD spectroscopy and thioflavine T fluorescence assay are presented. As a model peptide, the 11-28 fragment of Aβ was used. This model peptide is known to contain the core region responsible for Aβ aggregation. The structural and aggregational behaviour of the peptide was compared with the properties of its variants corresponding to natural, clinically relevant mutants at positions 21-23 (A21G, E22K, E22G, E22Q and D23N). In HFIP (hexafluoro-2-propanol), a strong α-helix inducer, the CD spectra revealed an unexpectedly high amount of β-sheet conformation. The aggregation process of Aβ(11-28) variants provoked by water addition to HFIP was found to be consistent with a model of an α-helix-containing intermediate. The aggregation propensity of all Aβ(11-28) variants was also compared and discussed.
Źródło:
Acta Biochimica Polonica; 2005, 52, 2; 425-431
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-2 z 2

    Ta witryna wykorzystuje pliki cookies do przechowywania informacji na Twoim komputerze. Pliki cookies stosujemy w celu świadczenia usług na najwyższym poziomie, w tym w sposób dostosowany do indywidualnych potrzeb. Korzystanie z witryny bez zmiany ustawień dotyczących cookies oznacza, że będą one zamieszczane w Twoim komputerze. W każdym momencie możesz dokonać zmiany ustawień dotyczących cookies