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Issue 39, 2019
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PrP (58–93) peptide from unstructured N-terminal domain of human prion protein forms amyloid-like fibrillar structures in the presence of Zn2+ ions

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Abstract

Many transition metal ions modulate the aggregation of different amyloid peptides. Substoichiometric zinc concentrations can inhibit aggregation, while an excess of zinc can accelerate the formation of cytotoxic fibrils. In this study, we report the fibrillization of the octarepeat domain to amyloid-like structures. Interestingly, this self-assembling process occurred only in the presence of Zn(II) ions. The formed peptide aggregates are able to bind amyloid specific dyes thioflavin T and Congo red. Atomic force microscopy and transmission electron microscopy revealed the formation of long, fibrillar structures. X-ray diffraction and Fourier transform infrared spectroscopy studies of the formed assemblies confirmed the presence of cross-β structure. Two-component analysis of synchrotron radiation SAXS data provided the evidence for a direct decrease in monomeric peptide species content and an increase in the fraction of aggregates as a function of Zn(II) concentration. These results could shed light on Zn(II) as a toxic agent and on the metal ion induced protein misfolding in prion diseases.

Graphical abstract: PrP (58–93) peptide from unstructured N-terminal domain of human prion protein forms amyloid-like fibrillar structures in the presence of Zn2+ ions

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Supplementary files

Article information


Submitted
27 Feb 2019
Accepted
07 Jul 2019
First published
17 Jul 2019

This article is Open Access

RSC Adv., 2019,9, 22211-22219
Article type
Paper

PrP (58–93) peptide from unstructured N-terminal domain of human prion protein forms amyloid-like fibrillar structures in the presence of Zn2+ ions

M. Gielnik, Z. Pietralik, I. Zhukov, A. Szymańska, W. M. Kwiatek and M. Kozak, RSC Adv., 2019, 9, 22211
DOI: 10.1039/C9RA01510H

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