Direct measurement of SARS-CoV-2 spike RBD binding to integrin α <sub>v</sub> β <sub>6</sub> by single-molecule force spectroscopy

Single-molecule force spectroscopy reveals strong, cation-dependent binding between SARS-CoV-2 RBD and integrin α<sub>v</sub>β<sub>6</sub>, with rupture forces exceeding those observed for ACE2, supporting integrin α<sub>v</sub>β<sub>6</sub> as an alternative receptor.

Authors

Peng Zheng (ORCID: https://orcid.org/0000-0003-4792-6364)
Bei Tong (ORCID: https://orcid.org/0000-0002-6863-6019)
F. Tian (ORCID: https://orcid.org/0000-0002-4212-6328)
Jiamin Li (ORCID: https://orcid.org/0009-0008-4112-7557)
Feng Tian (ORCID: https://orcid.org/0000-0003-2091-9412)
Xianchi Dong

Institutions

Institute of Botany (CN)
Nanjing University (CN)

Publication Details

Journal: Chemical Communications
Published: 2025-01-01
DOI: https://doi.org/10.1039/d5cc03034j
Citations: 1
Primary Topic: Lipid Membrane Structure and Behavior
Type: article
Field-Weighted Citation Impact: 0.81

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article

Direct measurement of SARS-CoV-2 spike RBD binding to integrin α _v β ₆ by single-molecule force spectroscopy

Peng Zheng, Bei Tong, F. Tian, Jiamin Li et al.

Jan 1, 2025

1 citations

Chemical Communications

Lipid Membrane Structure and Behavior

0.81

article

Direct measurement of SARS-CoV-2 spike RBD binding to integrin α _v β ₆ by single-molecule force spectroscopy

Peng Zheng, Bei Tong, F. Tian, Jiamin Li, Feng Tian, Xianchi Dong

January 1, 2025article en

1 citations

Abstract

Single-molecule force spectroscopy reveals strong, cation-dependent binding between SARS-CoV-2 RBD and integrin α<sub>v</sub>β<sub>6</sub>, with rupture forces exceeding those observed for ACE2, supporting integrin α<sub>v</sub>β<sub>6</sub> as an alternative receptor.

Chemical CommunicationsVol. 61(90)

Institute of Botany (CN), Nanjing University (CN)

Openalex Percentile: Top 25%

Lipid Membrane Structure and Behavior

0.81

DOI Source OpenAlex

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