Details
| Original language | English |
|---|---|
| Article number | 83 |
| Number of pages | 13 |
| Journal | Cells |
| Volume | 12 |
| Issue number | 1 |
| Publication status | Published - 25 Dec 2022 |
Abstract
Keywords
- ACE2, protein microarray, protein-protein interaction, SARS-CoV-2
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- General Biochemistry,Genetics and Molecular Biology
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In: Cells, Vol. 12, No. 1, 83, 25.12.2022.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Multiformin-Type Azaphilones Prevent SARS-CoV-2 Binding to ACE2 Receptor
AU - Jansen-Olliges, Linda
AU - Chatterjee, Shambhabi
AU - Jia, Lili
AU - Stahl, Frank
AU - Bär, Christian
AU - Stadler, Marc
AU - Surup, Frank
AU - Zeilinger, Carsten
N1 - Publisher Copyright: © 2022 by the authors.
PY - 2022/12/25
Y1 - 2022/12/25
N2 - Protein microarray screenings identified fungal natural products from the azaphilone family as potent inhibitors of SARS-CoV-2 spike protein binding to host ACE2 receptors. Cohaerin F, as the most potent substance from the cohaerin group, led to more than 50% less binding of ACE2 and SARS-CoV-2 spike protein. A survey for structurally related azaphilones yielded the structure elucidation of six new multiformins E–J (10–15) and the revision of the stereochemistry of the multiformins. Cohaerin and multiformin azaphilones (1–5, 8, 12) were assessed for their activity in a cell-based infection assay. Calu-3 cells expressing human ACE2 receptor showed more than 75% and 50% less infection by SARS-CoV-2 pseudotyped lentivirus particles after treatment with cohaerin C (1) and cohaerin F (4), respectively. Multiformin C (8) and G (12) that nearly abolished the infection of cells. Our data show that multiformin-type azaphilones prevent the binding of SARS-CoV-2 to the cell entry receptor ACE2.
AB - Protein microarray screenings identified fungal natural products from the azaphilone family as potent inhibitors of SARS-CoV-2 spike protein binding to host ACE2 receptors. Cohaerin F, as the most potent substance from the cohaerin group, led to more than 50% less binding of ACE2 and SARS-CoV-2 spike protein. A survey for structurally related azaphilones yielded the structure elucidation of six new multiformins E–J (10–15) and the revision of the stereochemistry of the multiformins. Cohaerin and multiformin azaphilones (1–5, 8, 12) were assessed for their activity in a cell-based infection assay. Calu-3 cells expressing human ACE2 receptor showed more than 75% and 50% less infection by SARS-CoV-2 pseudotyped lentivirus particles after treatment with cohaerin C (1) and cohaerin F (4), respectively. Multiformin C (8) and G (12) that nearly abolished the infection of cells. Our data show that multiformin-type azaphilones prevent the binding of SARS-CoV-2 to the cell entry receptor ACE2.
KW - ACE2
KW - protein microarray
KW - protein-protein interaction
KW - SARS-CoV-2
UR - http://www.scopus.com/inward/record.url?scp=85146029263&partnerID=8YFLogxK
U2 - 10.3390/cells12010083
DO - 10.3390/cells12010083
M3 - Article
VL - 12
JO - Cells
JF - Cells
SN - 2073-4409
IS - 1
M1 - 83
ER -