C-Terminal Fragment, Aβ39-42-Based Tetrapeptides Mitigates Amyloid-β Aggregation-Induced Toxicity.
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ABSTRACT: Since the introduction of acetyl cholinesterase inhibitors as the first approved drugs by the US Food and Drug Administration for Alzheimer's disease (AD) in clinics, less than satisfactory success in the design of anti-AD agents has impelled the scientists to also focus toward inhibition of Aβ aggregation. Considering the specific binding of fragments for their parent peptide, herein, we synthesized more than 40 new peptides based on a C-terminus tetrapeptide fragment of Aβ1-42. Initial screening by MTT cell viability assay and supportive results by ThT fluorescence assay led us to identify a tetrapeptide showing complete inhibition for Aβ1-42 aggregation. Peptide 20 displayed 100% cell viability at 20 μM concentration, while at lower concentrations of 10 and
SUBMITTER: Bansal S
PROVIDER: S-EPMC6645473 | biostudies-literature | 2018 Aug
REPOSITORIES: biostudies-literature
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