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

DOI: 10.1021/acsnano.1c10658 DOI Help

Authors: Valeria Castelletto (University of Reading) , Ian W. Hamley (University of Reading)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acs Nano , VOL 1777

State: Published (Approved)
Published: January 2022
Diamond Proposal Number(s): 28659

Open Access Open Access

Abstract: 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.

Journal Keywords: amyloid; coronavirus; spike protein; nanotapes; aggregation; hydrogels

Diamond Keywords: COVID-19; Viruses

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: B21-High Throughput SAXS

Other Facilities: BM29 at ESRF

Added On: 05/01/2022 15:36

Documents:
acsnano.1c10658.pdf

Discipline Tags:

Pathogens Infectious Diseases Health & Wellbeing Biochemistry Chemistry Structural biology Life Sciences & Biotech

Technical Tags:

Scattering Small Angle X-ray Scattering (SAXS)