Amyloid and hydrogel formation of a peptide sequence from a coronavirus spike protein

Castelletto, V. ORCID: https://orcid.org/0000-0002-3705-0162 and Hamley, I. W. ORCID: https://orcid.org/0000-0002-4549-0926 (2022) Amyloid and hydrogel formation of a peptide sequence from a coronavirus spike protein. ACS Nano, 16 (2). pp. 1857-1867. ISSN 1936-086X doi: 10.1021/acsnano.1c10658

Abstract/Summary

We demonstrate that a conserved coronavirus spike protein peptide forms amyloid structures, differing from the native helical conformation and not predicted by amyloid aggregation algorithms. We investigate the conformation and aggregation of peptide RSAIEDLLFDKV, which is a sequence common to many animal and human coronavirus spike proteins. This sequence is part of a native α-helical S2 glycoprotein domain, close to and partly spanning the fusion sequence. This peptide aggregates into β-sheet amyloid nanotape structures close to the calculated pI = 4.2, but forms disordered monomers at high and low pH. The β-sheet conformation revealed by FTIR and circular dichroism (CD) spectroscopy leads to peptide nanotape structures, imaged using transmission electron microscopy (TEM) and probed by small-angle X-ray scattering (SAXS). The nanotapes comprise arginine-coated bilayers. A Congo red dye UV–vis assay is used to probe the aggregation of the peptide into amyloid structures, which enabled the determination of a critical aggregation concentration (CAC). This peptide also forms hydrogels under precisely defined conditions of pH and concentration, the rheological properties of which were probed. The observation of amyloid formation by a coronavirus spike has relevance to the stability of the spike protein conformation (or its destabilization via pH change), and the peptide may have potential utility as a functional material. Hydrogels formed by coronavirus peptides may also be of future interest in the development of slow-release systems, among other applications.

Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/102161
Identification Number/DOI	10.1021/acsnano.1c10658
Refereed	Yes
Divisions	Interdisciplinary centres and themes > Chemical Analysis Facility (CAF) Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry Interdisciplinary centres and themes > Chemical Analysis Facility (CAF) > Electron Microscopy Laboratory (CAF)
Publisher	American Chemical Society
Download/View statistics	View download statistics for this item