Mass photometry reveals SARS-CoV-2 spike stabilisation to impede ACE2 binding through altered conformational dynamics

Sean A. Burnap; Weston B. Struwe

doi:10.1039/d2cc04711j

journal article Open Access Jan 01, 2022

Mass photometry reveals SARS-CoV-2 spike stabilisation to impede ACE2 binding through altered conformational dynamics

Sean A. Burnap

Weston B. Struwe

Chemical Communications Vol. 58 No. 93 pp. 12939-12942 · Royal Society of Chemistry (RSC)

View at Publisher Save 10.1039/d2cc04711j

Abstract

Here we show using mass photometry how proline substitutions, commonly used for SARS-CoV-2 spike stabilisation in vaccine design, directly affects ACE2 receptor interactions via dynamics of open and closed states.

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Citations

13

References

Details

Published: Jan 01, 2022
Vol/Issue: 58(93)
Pages: 12939-12942
License: View

Authors

S

Sean A. Burnap

Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, OX1 3TA, UK; The Kavli Institute for Nanoscience Discovery, Dorothy Crowfoot Hodgkin Building, South Parks Road, OX1 3QU, UK

W

Weston B. Struwe

Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, OX1 3TA, UK; The Kavli Institute for Nanoscience Discovery, Dorothy Crowfoot Hodgkin Building, South Parks Road, OX1 3QU, UK

Funding

Biotechnology and Biological Sciences Research Council Award: BBSRC/UKRI BB/V011456/1

UK Research and Innovation Award: MR/V02213X/1

Cite This Article

Sean A. Burnap, Weston B. Struwe (2022). Mass photometry reveals SARS-CoV-2 spike stabilisation to impede ACE2 binding through altered conformational dynamics. Chemical Communications, 58(93), 12939-12942. https://doi.org/10.1039/d2cc04711j

Mass photometry reveals SARS-CoV-2 spike stabilisation to impede ACE2 binding through altered conformational dynamics

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