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    Functionalized fullerene for inhibition of SARS-CoV-2 variants (2023)

    Art
    Zeitschriftenartikel / wissenschaftlicher Beitrag
    Autoren
    Page, Taylor M.
    Nie, Chuanxiong
    Neander, Lenard
    Povolotsky, Tatyana L.
    Sahoo, Anil Kumar
    Nickl, Philip
    Adler, Julia M. (WE 5)
    Bawadkji, Obida
    Radnik, Jörg
    Achazi, Katharina
    Ludwig, Kai
    Lauster, Daniel
    Netz, Roland R.
    Trimpert, Jakob (WE 5)
    Kaufer, Benedikt (WE 5)
    Haag, Rainer
    Donskyi, Ievgen S.
    Quelle
    Small : nano micro
    Bandzählung: 19
    Heftzählung: 15
    Seiten: Artikel 2206154
    ISSN: 1613-6829
    Sprache
    Englisch
    Verweise
    URL (Volltext): https://onlinelibrary.wiley.com/doi/10.1002/smll.202206154
    DOI: 10.1002/smll.202206154
    Pubmed: 36651127
    Kontakt
    Institut für Virologie

    Robert-von-Ostertag-Str. 7-13
    14163 Berlin
    +49 30 838 51833
    virologie@vetmed.fu-berlin.de

    Abstract / Zusammenfassung

    As virus outbreaks continue to pose a challenge, a nonspecific viral inhibitor can provide significant benefits, especially against respiratory viruses. Polyglycerol sulfates recently emerge as promising agents that mediate interactions between cells and viruses through electrostatics, leading to virus inhibition. Similarly, hydrophobic C60 fullerene can prevent virus infection via interactions with hydrophobic cavities of surface proteins. Here, two strategies are combined to inhibit infection of SARS-CoV-2 variants in vitro. Effective inhibitory concentrations in the millimolar range highlight the significance of bare fullerene's hydrophobic moiety and electrostatic interactions of polysulfates with surface proteins of SARS-CoV-2. Furthermore, microscale thermophoresis measurements support that fullerene linear polyglycerol sulfates interact with the SARS-CoV-2 virus via its spike protein, and highlight importance of electrostatic interactions within it. All-atom molecular dynamics simulations reveal that the fullerene binding site is situated close to the receptor binding domain, within 4 nm of polyglycerol sulfate binding sites, feasibly allowing both portions of the material to interact simultaneously.