β-Turn mimetic synthetic peptides as amyloid-β aggregation inhibitors
نویسندگان
چکیده
منابع مشابه
Synthesis and biological assessment of 2-hydroxyiminoethanones as anti-inflammatory and β-amyloid aggregation inhibitors
Alzheimer’s disease (AD) is a neuroinflammatory based pathologic state in which β-amyloid aggregates are a major devastating agents. In this study, a series of 2-hydroxyiminoethanones were synthesized and evaluated as anti-inflammatory in carrageenan and formalin tests and inhibitors of β-amyloid aggregation. Compounds 1-10b were synthesized through a two-step reaction. Results: Compounds 1-5b ...
متن کاملSynthesis and biological assessment of 2-hydroxyiminoethanones as anti-inflammatory and β-amyloid aggregation inhibitors
Alzheimer’s disease (AD) is a neuroinflammatory based pathologic state in which β-amyloid aggregates are a major devastating agents. In this study, a series of 2-hydroxyiminoethanones were synthesized and evaluated as anti-inflammatory in carrageenan and formalin tests and inhibitors of β-amyloid aggregation. Compounds 1-10b were synthesized through a two-step reaction. Results: Compounds 1-5b ...
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Modulation of abnormal amyloid β (Aβ) aggregation is considered to be a potential therapeutic target for Alzheimer's disease (AD). Recent in vitro and in vivo experiments suggest that inhibition of Aβ aggregation by curcumin would exert favorable effects for preventing or treating AD. We have previously synthesized a series of novel curcumin derivatives. In this study, we investigated the effec...
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The misfolding and aggregation of proteins into amyloid has been linked to a variety of age-related diseases. Aggregation of proteins, such as Aβ in Alzheimer's disease and Islet Amyloid Polypeptide (IAPP, amylin) in type 2 diabetes, appears to lead to the formation of toxic assemblies. These assemblies range in size from small oligomers (2-8 proteins) to large fibrils (thousands of proteins). ...
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Pathogenesis of Alzheimer's disease (AD) is associated with aggregation of the amyloid-β (Aβ) peptide into oligomeric and fibrillar assemblies; however, little is known about the molecular basis of aggregation of Aβ into distinct assembly states. Here we demonstrate that phosphorylation at serine 26 (S26) impairs Aβ fibrillization while stabilizing its monomers and nontoxic soluble assemblies o...
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ژورنال
عنوان ژورنال: Bioorganic Chemistry
سال: 2020
ISSN: 0045-2068
DOI: 10.1016/j.bioorg.2020.104012