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Structure and Orientation of the SARS-Coronavirus-2 Spike Protein at Air-Water Interfaces.
Bregnhøj, Mikkel; Roeters, Steven J; Chatterley, Adam S; Madzharova, Fani; Mertig, Rolf; Pedersen, Jan Skov; Weidner, Tobias.
  • Bregnhøj M; Department of Chemistry, Aarhus University, Langelandsgade 140, 8000 Aarhus C, Denmark.
  • Roeters SJ; Department of Chemistry, Aarhus University, Langelandsgade 140, 8000 Aarhus C, Denmark.
  • Chatterley AS; Department of Chemistry, Aarhus University, Langelandsgade 140, 8000 Aarhus C, Denmark.
  • Madzharova F; Department of Chemistry, Aarhus University, Langelandsgade 140, 8000 Aarhus C, Denmark.
  • Mertig R; Department of Chemistry, Aarhus University, Langelandsgade 140, 8000 Aarhus C, Denmark.
  • Pedersen JS; Department of Chemistry, Aarhus University, Langelandsgade 140, 8000 Aarhus C, Denmark.
  • Weidner T; Department of Chemistry, Aarhus University, Langelandsgade 140, 8000 Aarhus C, Denmark.
J Phys Chem B ; 126(18): 3425-3430, 2022 05 12.
Article in English | MEDLINE | ID: covidwho-1815470
ABSTRACT
The SARS coronavirus 2 (SARS-CoV-2) spike protein is located at the outermost perimeter of the viral envelope and is the first component of the virus to make contact with surrounding interfaces. The stability of the spike protein when in contact with surfaces plays a deciding role for infection pathways and for the viability of the virus after surface contact. While cryo-EM structures of the spike protein have been solved with high resolution and structural studies in solution have provided information about the secondary and tertiary structures, only little is known about the folding when adsorbed to surfaces. We here report on the secondary structure and orientation of the S1 segment of the spike protein, which is often used as a model protein for in vitro studies of SARS-CoV-2, at the air-water interface using surface-sensitive vibrational sum-frequency generation (SFG) spectroscopy. The air-water interface plays an important role for SARS-CoV-2 when suspended in aerosol droplets, and it serves as a model system for hydrophobic surfaces in general. The SFG experiments show that the S1 segment of the spike protein remains folded at the air-water interface and predominantly binds in its monomeric state, while the combination of small-angle X-ray scattering and two-dimensional infrared spectroscopy measurements indicate that it forms hexamers with the same secondary structure in aqueous solution.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 Limits: Humans Language: English Journal: J Phys Chem B Journal subject: Chemistry Year: 2022 Document Type: Article Affiliation country: Acs.jpcb.2c01272

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Full text: Available Collection: International databases Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 Limits: Humans Language: English Journal: J Phys Chem B Journal subject: Chemistry Year: 2022 Document Type: Article Affiliation country: Acs.jpcb.2c01272