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    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:
    Dobry amyloid β? Właściwości chemiczne peptydów Aβ4-x wskazują na ich znaczenie biologiczne
    Good β-amyloid? Chemical properties of Aβ4-x peptides indicate their biological relevance
    Autorzy:
    Bal, Wojciech
    Powiązania:
    https://bibliotekanauki.pl/articles/172163.pdf
    Data publikacji:
    2019
    Wydawca:
    Polskie Towarzystwo Chemiczne
    Tematy:
    peptydy β-amyloidowe
    choroba Alzheimera
    ATCUN/NTS
    wiązanie Cu(II)
    aktywność redoks
    amyloid β peptides
    Alzheimer’s disease
    Cu(II) binding
    redox reactivity
    Opis:
    Alzheimer’s Disease is a neurodegenerative condition, an irreversible progressive dementia caused by death of neurons in brain structures responsible for memory related processes. Despite many years of research and numerous trials, no therapy succeeded that could stop the development of this disease, which affects tens of millions of patients worldwide. The amyloid cascade prevails among a variety of possible mechanisms of its development proposed in the scientific literature. It proposes that death of neurons, preceded by dysfunction of their synaptic activity is caused by the incremental formation of structures (fibrils, oligomers) composed of Aβ peptides. In its copper variant the processes of aggregation and oxidative stress, causing the inflammation and neuronal damage are related to the formation of reactive Cu(II) complexes with Aβ peptides. Aβ peptides are a family of molecules with similar amino acid sequences, differing mainly by the presence of longer or shorter terminal sequences. Their physiological role of is unclear. Aβ1-42 and Aβ1-40 have been mostly studied, but most studies have ignored a very abundant N-terminally truncated species Aβ4-42. We recognized it, and more gene-rally the Aβ4-x peptide family as potentially strong Cu(II) ligands, due to the presence at their N-termini of the Phe-Arg-His amino acid sequence, comprising the ATCUN/NTS structural motif. This observation was followed by vigorous research performed in our laboratory. We studied the ability of Aβ4-x peptides to bind Cu(II) ions, their electrochemical properties and redox reactivity, interactions with proteins which bind copper under physiological conditions, their aggregation properties in the Cu(II) presence and susceptibility to proteolysis. Additionally, we investigated their interaction with a molecule of a therapeutic potential. We demonstrated that Aβ4-x peptides can be primary copper bin-ding agents in extracellular spaces in the brain, able to instantaneously intercept copper from Aβ1-x peptides studied so far. Cu(II) complexes of Aβ4-x peptides are highly resistant to oxidation and reduction, release copper ions to other molecules slowly and reluctantly, and do not produce reactive oxygen species. In accordance with these properties we proposed a physiological role for the Aβ4-42 peptide as a molecule cleansing the synaptic cleft from Cu2+ ions and thereby assuring the correct neurotransmission. This function can however be disturbed by an inappropriate pharmacological intervention. The results of studies of the effect of cupric ions on the aggregation and membrane interactions of the Aβ4-40 peptides suggest that copper can inhibit the Aβ4-x peptides toxicity, thereby providing an additional support for our concept. Studies of hydrolysis of Aβ peptides and properties of its products revealed a possibility for a significant role of short fragments in the brain copper physiology. Our hypothesis awaits verification by biological studies. The issue of metabolism of the studied complexes is a key issue remaining to be solved.
    Źródło:
    Wiadomości Chemiczne; 2019, 73, 5-6; 351-366
    0043-5104
    2300-0295
    Pojawia się w:
    Wiadomości Chemiczne
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-2 z 2

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