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- W2066349973 startingPage "991" @default.
- W2066349973 abstract "Hen egg white lysozyme (HEWL) adopts a molten globule-like state at high pH (~12.75) and is found to form amyloid fibrils at alkaline pH. Here, we report that Cu(II) inhibits self-association of HEWL at pH 12.75 both at 37 and 65 °C. A significant reduction in Thioflavin T fluorescence intensity, attenuation in β-sheet content and reduction in hydrophobic exposure were observed with increasing Cu(II) stoichiometry. Electron paramagnetic resonance spectroscopy suggests a 4N type of coordination pattern around Cu(II) during fibrillation. Cu(II) is also capable of altering the cytotoxicity of the proteinaceous aggregates. Fibrillar species of diverse morphology were found in the absence of Cu(II) with the generation of amorphous aggregates in the presence of Cu(II), which are more toxic compared to the fibrils alone." @default.
- W2066349973 created "2016-06-24" @default.
- W2066349973 creator A5003186673 @default.
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- W2066349973 creator A5034456036 @default.
- W2066349973 creator A5043072965 @default.
- W2066349973 creator A5076665271 @default.
- W2066349973 date "2014-05-28" @default.
- W2066349973 modified "2023-10-18" @default.
- W2066349973 title "Copper(II) directs formation of toxic amorphous aggregates resulting in inhibition of hen egg white lysozyme fibrillation under alkaline salt-mediated conditions" @default.
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- W2066349973 doi "https://doi.org/10.1080/07391102.2014.921864" @default.
- W2066349973 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24806136" @default.
- W2066349973 hasPublicationYear "2014" @default.