From the journal:

Chemical Communications

Direct measurement of SARS-CoV-2 spike RBD binding to integrin αvβ6 by single-molecule force spectroscopy

Tianfu Feng,†a   Fang Tian,†a   Jiamin Li,†a   Xianchi Dong,b   Bei Tong*c  and  Peng Zheng ORCID logo *a  

* Corresponding authors

a State Key Laboratory of Coordination Chemistry, School of Chemistry and Chemical Engineering, Chemistry and Biomedicine Innovation Centre (ChemBIC), Nanjing University, Nanjing, P. R. China
E-mail: pengz@nju.edu.cn

b State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Nanjing, P. R. China

c Jiangsu Key Laboratory for Conservation and Utilization of Plant Resources, Institute of Botany, Jiangsu Province and Chinese Academy of Sciences (Nanjing Botanical Garden Memorial Sun Yat-Sen), Nanjing 210014, P. R. China
E-mail: beitong@cnbg.net

Abstract

Single-molecule force spectroscopy reveals strong, cation-dependent binding between SARS-CoV-2 RBD and integrin αvβ6, with rupture forces exceeding those observed for ACE2, supporting integrin αvβ6 as an alternative receptor.

Graphical abstract: Direct measurement of SARS-CoV-2 spike RBD binding to integrin αvβ6 by single-molecule force spectroscopy

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Article information

DOI
https://doi.org/10.1039/D5CC03034J
Article type
Communication
Submitted
29 May 2025
Accepted
29 Jul 2025
First published
29 Jul 2025

Chem. Commun., 2025, Advance Article

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Direct measurement of SARS-CoV-2 spike RBD binding to integrin αvβ6 by single-molecule force spectroscopy

T. Feng, F. Tian, J. Li, X. Dong, B. Tong and P. Zheng, Chem. Commun., 2025, Advance Article , DOI: 10.1039/D5CC03034J

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