Adsorption of SARS‐CoV‐2 Spike Protein S1 at Oxide Surfaces Studied by High‐Speed Atomic Force Microscopy

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Biointerfaces The cover image shows the adsorption of SARS‐CoV‐2 at metal‐based fomite surfaces. The spike protein subunit S1 is the outermost point of the viral envelope and thus mediates the initial contact between the virus and the fomite surface. High‐speed atomic force microscopy movies reveal...

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Detalles Bibliográficos
Autores principales: Xin, Yang, Grundmeier, Guido, Keller, Adrian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Back Cover
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7994987/
https://www.ncbi.nlm.nih.gov/pubmed/33786537
http://dx.doi.org/10.1002/anbr.202170023
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author Xin, Yang
Grundmeier, Guido
Keller, Adrian
author_facet Xin, Yang
Grundmeier, Guido
Keller, Adrian
author_sort Xin, Yang
collection PubMed
description Biointerfaces The cover image shows the adsorption of SARS‐CoV‐2 at metal‐based fomite surfaces. The spike protein subunit S1 is the outermost point of the viral envelope and thus mediates the initial contact between the virus and the fomite surface. High‐speed atomic force microscopy movies reveal that S1 protein adsorption proceeds faster at TiO(2) surfaces than at Al(2)O(3) surfaces. More details can be found in article number 2000024 by Adrian Keller and co‐workers [Image: see text]
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spelling pubmed-79949872021-03-26 Adsorption of SARS‐CoV‐2 Spike Protein S1 at Oxide Surfaces Studied by High‐Speed Atomic Force Microscopy Xin, Yang Grundmeier, Guido Keller, Adrian Adv Nanobiomed Res Back Cover Biointerfaces The cover image shows the adsorption of SARS‐CoV‐2 at metal‐based fomite surfaces. The spike protein subunit S1 is the outermost point of the viral envelope and thus mediates the initial contact between the virus and the fomite surface. High‐speed atomic force microscopy movies reveal that S1 protein adsorption proceeds faster at TiO(2) surfaces than at Al(2)O(3) surfaces. More details can be found in article number 2000024 by Adrian Keller and co‐workers [Image: see text] John Wiley and Sons Inc. 2021-02-05 2021-02 /pmc/articles/PMC7994987/ /pubmed/33786537 http://dx.doi.org/10.1002/anbr.202170023 Text en © 2021 Wiley‐VCH GmbH https://creativecommons.org/licenses/by-nc/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.
spellingShingle Back Cover
Xin, Yang
Grundmeier, Guido
Keller, Adrian
Adsorption of SARS‐CoV‐2 Spike Protein S1 at Oxide Surfaces Studied by High‐Speed Atomic Force Microscopy
title Adsorption of SARS‐CoV‐2 Spike Protein S1 at Oxide Surfaces Studied by High‐Speed Atomic Force Microscopy
title_full Adsorption of SARS‐CoV‐2 Spike Protein S1 at Oxide Surfaces Studied by High‐Speed Atomic Force Microscopy
title_fullStr Adsorption of SARS‐CoV‐2 Spike Protein S1 at Oxide Surfaces Studied by High‐Speed Atomic Force Microscopy
title_full_unstemmed Adsorption of SARS‐CoV‐2 Spike Protein S1 at Oxide Surfaces Studied by High‐Speed Atomic Force Microscopy
title_short Adsorption of SARS‐CoV‐2 Spike Protein S1 at Oxide Surfaces Studied by High‐Speed Atomic Force Microscopy
title_sort adsorption of sars‐cov‐2 spike protein s1 at oxide surfaces studied by high‐speed atomic force microscopy
topic Back Cover
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7994987/
https://www.ncbi.nlm.nih.gov/pubmed/33786537
http://dx.doi.org/10.1002/anbr.202170023
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AT kelleradrian adsorptionofsarscov2spikeproteins1atoxidesurfacesstudiedbyhighspeedatomicforcemicroscopy

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