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Fusion Peptide of SARS-CoV-2 Spike Rearranges into a Wedge Inserted in Bilayered Micelles

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    Fusion Peptide of SARS-CoV-2 Spike Rearranges into a Wedge Inserted in Bilayered Micelles
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    • Rama K. Koppisetti
      Rama K. Koppisetti
      Department of Biochemistry, University of Missouri, Columbia, Missouri 65211 United States
      More by Rama K. Koppisetti
    • Yan G. Fulcher
      Yan G. Fulcher
      Department of Biochemistry, University of Missouri, Columbia, Missouri 65211 United States
      More by Yan G. Fulcher
    • Steven R. Van Doren*
      Steven R. Van Doren
      Department of Biochemistry, University of Missouri, Columbia, Missouri 65211 United States
      Institute for Data Science and Informatics, University of Missouri, Columbia, Missouri 65211 United States
      *Email: [email protected]
      More by Steven R. Van Doren
      Orcidhttps://orcid.org/0000-0003-2838-4598
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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2021, 143, 33, 13205–13211
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    https://doi.org/10.1021/jacs.1c05435
    Published August 10, 2021
    Copyright © 2021 American Chemical Society
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    The receptor binding and proteolysis of Spike of SARS-CoV-2 release its S2 subunit to rearrange and catalyze viral-cell fusion. This deploys the fusion peptide for insertion into the cell membranes targeted. We show that this fusion peptide transforms from intrinsic disorder in solution into a wedge-shaped structure inserted in bilayered micelles, according to chemical shifts, 15N NMR relaxation, and NOEs. The globular fold of three helices contrasts the open, extended forms of this region observed in the electron density of compact prefusion states. In the hydrophobic, narrow end of the wedge, helices 1 and 2 contact the fatty acyl chains of phospholipids, according to NOEs and proximity to a nitroxide spin label deep in the membrane mimic. The polar end of the wedge may engage and displace lipid head groups and bind Ca2+ ions for membrane fusion. Polar helix 3 protrudes from the bilayer where it might be accessible to antibodies.

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    Cite this: J. Am. Chem. Soc. 2021, 143, 33, 13205–13211
    Click to copy citationCitation copied!
    https://doi.org/10.1021/jacs.1c05435
    Published August 10, 2021
    Copyright © 2021 American Chemical Society
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