Copper(II) directs formation of toxic amorphous aggregates resulting in inhibition of hen egg white lysozyme fibrillation under alkaline salt-mediated conditions

Ghosh, Sudeshna ; Pandey, Nitin K. ; Banerjee, Priyanka ; Chaudhury, Koel ; Nagy, Nora Veronika ; Dasgupta, Swagata (2014) Copper(II) directs formation of toxic amorphous aggregates resulting in inhibition of hen egg white lysozyme fibrillation under alkaline salt-mediated conditions Journal of Biomolecular Structure and Dynamics, 33 (5). pp. 991-1007. ISSN 0739-1102

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Official URL: https://www.tandfonline.com/doi/10.1080/07391102.2...

Related URL: http://dx.doi.org/10.1080/07391102.2014.921864

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.

Item Type:Article
Source:Copyright of this article belongs to Taylor and Francis Group.
Keywords:Hen Egg White Lysozyme; Molten Globule State; Fibrillation; Cu(II) Stoichiometry; Inhibition; Cytotoxicity
ID Code:112843
Deposited On:10 May 2018 11:20
Last Modified:10 May 2018 11:20

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