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1.
Eur J Cancer Care (Engl) ; 31(6): e13657, 2022 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-35838182

RESUMO

OBJECTIVES: The COVID-19 pandemic's ongoing effects and long-term implications for the mental and social state of cancer patients are not yet fully known. The current study examined cancer patients' feelings about the pandemic's long-term impact on daily life 1 year after its outbreak in Israel and after the patient's vaccination against the virus. METHODS: Ten in-depth semi-structured interviews were conducted with cancer patients between February and April 2021. RESULTS AND CONCLUSIONS: Findings indicated four main themes: (1) managing medical care and support from the medical staff, (2) the effect of the pandemic on social interactions; (3) the impact of the pandemic on family and social support and (4) the patients' psychological well-being. Despite the patients being vaccinated, the full impact of the pandemic on cancer patients' mental and social states is still fully apparent. The findings reflect the need to assess and monitor the patients' mental state and social and medical needs during this complex time and the importance of developing external support networks.


Assuntos
COVID-19 , Neoplasias , Humanos , Pandemias , Israel/epidemiologia , Pesquisa Qualitativa , Neoplasias/terapia
2.
ACS Chem Neurosci ; 14(18): 3385-3397, 2023 09 20.
Artigo em Inglês | MEDLINE | ID: mdl-37579500

RESUMO

An amyloid precursor protein inhibitor (APPI) and amyloid beta 42 (Aß42) are both subdomains of the human transmembrane amyloid precursor protein (APP). In the brains of patients with Alzheimer's disease (AD), Aß42 oligomerizes into aggregates of various sizes, with intermediate, low-molecular-weight Aß42 oligomers currently being held to be the species responsible for the most neurotoxic effects associated with the disease. Strategies to ameliorate the toxicity of these intermediate Aß42 oligomeric species include the use of short, Aß42-interacting peptides that either inhibit the formation of the Aß42 oligomeric species or promote their conversion to high-molecular-weight aggregates. We therefore designed such an Aß42-interacting peptide that is based on the ß-hairpin amino acid sequence of the APPI, which exhibits high similarity to the ß-sheet-like aggregation site of Aß42. Upon tight binding of this 20-mer cyclic peptide to Aß42 (in a 1:1 molar ratio), the formation of Aß42 aggregates was enhanced, and consequently, Aß42-mediated cell toxicity was ameliorated. We showed that in the presence of the cyclic peptide, interactions of Aß42 with both plasma and mitochondrial membranes and with phospholipid vesicles that mimic these membranes were inhibited. Specifically, the cyclic peptide inhibited Aß42-mediated mitochondrial membrane depolarization and reduced Aß42-mediated apoptosis and cell death. We suggest that the cyclic peptide modulates Aß42 aggregation by enhancing the formation of large aggregates─as opposed to low-molecular-weight intermediates─and as such has the potential for further development as an AD therapeutic.


Assuntos
Doença de Alzheimer , Peptídeos beta-Amiloides , Humanos , Peptídeos beta-Amiloides/metabolismo , Precursor de Proteína beta-Amiloide , Peptídeos Cíclicos/farmacologia , Fragmentos de Peptídeos/metabolismo , Doença de Alzheimer/metabolismo
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