Medicine and Health

Molecular interaction and inhibition of SARS-CoV-2 binding to the ACE2 receptor

J. Yang, S. J. L. Petitjean, et al.

This study reveals the intricate binding mechanism of SARS-CoV-2 spike glycoprotein to the ACE2 receptor using atomic force microscopy. The researchers identify the receptor-binding domain as the key interaction site and explore potential peptide inhibitors for therapeutic applications, conducted by Jinsung Yang, Simon J. L. Petitjean, Melanie Koehler, Qingrong Zhang, Andra C. Dumitru, Wenzhang Chen, Sylvie Declercq, Stéphane P. Vincent, Patrice Soumillion, and David Alsteens.

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Abstract

This study investigates the binding mechanism of SARS-CoV-2 spike glycoprotein (S-glycoprotein) to the ACE2 receptor using atomic force microscopy (AFM). The researchers demonstrate that the receptor-binding domain (RBD) within the S-glycoprotein is the primary binding interface with ACE2. They extract kinetic and thermodynamic properties of this interaction both on model surfaces and living cells. Finally, they test several ACE2-derived peptides as potential binding inhibitors, offering new therapeutic perspectives for SARS-CoV-2 infection.

Publisher

Nature Communications

Published On

Sep 11, 2020

Authors

Jinsung Yang, Simon J. L. Petitjean, Melanie Koehler, Qingrong Zhang, Andra C. Dumitru, Wenzhang Chen, Sylvie Declercq, Stéphane P. Vincent, Patrice Soumillion, David Alsteens

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