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Issue 31, 2020
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Quantitative determination of mechanical stability in the novel coronavirus spike protein

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Abstract

We report on the novel observation about the gain in nanomechanical stability of the SARS-CoV-2 (CoV2) spike (S) protein in comparison with SARS-CoV from 2002 (CoV1). Our findings have several biological implications in the subfamily of coronaviruses, as they suggest that the receptor binding domain (RBD) (∼200 amino acids) plays a fundamental role as a damping element of the massive viral particle's motion prior to cell-recognition, while also facilitating viral attachment, fusion and entry. The mechanical stability via pulling of the RBD is 250 pN and 200 pN for CoV2 and CoV1 respectively, and the additional stability observed for CoV2 (∼50 pN) might play a role in the increasing spread of COVID-19.

Graphical abstract: Quantitative determination of mechanical stability in the novel coronavirus spike protein

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Article information


Submitted
23 May 2020
Accepted
22 Jul 2020
First published
23 Jul 2020

Nanoscale, 2020,12, 16409-16413
Article type
Communication

Quantitative determination of mechanical stability in the novel coronavirus spike protein

R. A. Moreira, M. Chwastyk, J. L. Baker, H. V. Guzman and A. B. Poma, Nanoscale, 2020, 12, 16409
DOI: 10.1039/D0NR03969A

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