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Fullerenes against COVID-19: Repurposing C60 and C70 to Clog the Active Site of SARS-CoV-2 Protease.
Marforio, Tainah Dorina; Mattioli, Edoardo Jun; Zerbetto, Francesco; Calvaresi, Matteo.
  • Marforio TD; Dipartimento di Chimica "Giacomo Ciamician", Alma Mater Studiorum-Università di Bologna, Via Francesco Selmi 2, 40126 Bologna, Italy.
  • Mattioli EJ; Dipartimento di Chimica "Giacomo Ciamician", Alma Mater Studiorum-Università di Bologna, Via Francesco Selmi 2, 40126 Bologna, Italy.
  • Zerbetto F; Dipartimento di Chimica "Giacomo Ciamician", Alma Mater Studiorum-Università di Bologna, Via Francesco Selmi 2, 40126 Bologna, Italy.
  • Calvaresi M; Dipartimento di Chimica "Giacomo Ciamician", Alma Mater Studiorum-Università di Bologna, Via Francesco Selmi 2, 40126 Bologna, Italy.
Molecules ; 27(6)2022 Mar 16.
Article in English | MEDLINE | ID: covidwho-1742559
ABSTRACT
The persistency of COVID-19 in the world and the continuous rise of its variants demand new treatments to complement vaccines. Computational chemistry can assist in the identification of moieties able to lead to new drugs to fight the disease. Fullerenes and carbon nanomaterials can interact with proteins and are considered promising antiviral agents. Here, we propose the possibility to repurpose fullerenes to clog the active site of the SARS-CoV-2 protease, Mpro. Through the use of docking, molecular dynamics, and energy decomposition techniques, it is shown that C60 has a substantial binding energy to the main protease of the SARS-CoV-2 virus, Mpro, higher than masitinib, a known inhibitor of the protein. Furthermore, we suggest the use of C70 as an innovative scaffold for the inhibition of SARS-CoV-2 Mpro. At odds with masitinib, both C60 and C70 interact more strongly with SARS-CoV-2 Mpro when different protonation states of the catalytic dyad are considered. The binding of fullerenes to Mpro is due to shape complementarity, i.e., vdW interactions, and is aspecific. As such, it is not sensitive to mutations that can eliminate or invert the charges of the amino acids composing the binding pocket. Fullerenic cages should therefore be more effective against the SARS-CoV-2 virus than the available inhibitors such as masinitib, where the electrostatic term plays a crucial role in the binding.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Fullerenes / COVID-19 Drug Treatment Type of study: Prognostic study Topics: Vaccines / Variants Limits: Humans Language: English Journal subject: Biology Year: 2022 Document Type: Article Affiliation country: Molecules27061916

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Fullerenes / COVID-19 Drug Treatment Type of study: Prognostic study Topics: Vaccines / Variants Limits: Humans Language: English Journal subject: Biology Year: 2022 Document Type: Article Affiliation country: Molecules27061916