Amyloid and Hydrogel Formation of a Peptide Sequence from a Coronavirus Spike Protein

Valeria Casteletto, Ian W. Hamley

Amyloid and Hydrogel Formation of a Peptide Sequence from a Coronavirus Spike Protein

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 … This peptide also forms hydrogels under precisely defined conditions of pH and concentration, the rheological properties of which were probed.


Latest articles

Joseph Mercola The U.S. population, aged 16 years and over, with a...
Joseph Mercola The rate of COVID-19 associated hospitalization among children aged 5...
Bhaskaran Raman A study titled “Global impact of the first year of COVID-19...
Randy L. Gollub Imaging before and after infection by the SARS-CoV-2 virus...
Einar Stefánsson et al. A natural component of fish oils, free fatty...
Jessica Rose Because: Safe and Effective. Foreverrrrrrrrururrrurururrr This is the meeting [VRBPAC...

Your donation helps us
stand up for health freedom!

Canada Health Alliance is volunteer run and 100% supported by the generous donations of those who share our concerns and value our work.

Stay up to date

Sign up to our newsletter to get the latest health-related news and events delivered straight to your inbox.

Become a CHA member

Become an active value-added member and trusted provider of medical and healthcare information and education by joining the CHA Membership Program.

Your donation helps us stand up for health freedom!

Canada Health Alliance is volunteer run and 100% supported by the generous donations of those who share our concerns and value our work.