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Adsorption of SARS‐CoV‐2 Spike Protein S1 at Oxide Surfaces Studied by High‐Speed Atomic Force Microscopy
Author(s) -
Xin Yang,
Grundmeier Guido,
Keller Adrian
Publication year - 2021
Publication title -
advanced nanobiomed research
Language(s) - English
Resource type - Journals
ISSN - 2699-9307
DOI - 10.1002/anbr.202170023
Subject(s) - adsorption , envelope (radar) , spike protein , atomic force microscopy , covid-19 , oxide , nanotechnology , materials science , chemistry , computer science , medicine , telecommunications , radar , disease , pathology , infectious disease (medical specialty) , metallurgy
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

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