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SARS-CoV-2 inhibitory activity of a short peptide derived from internal fusion peptide of S2 subunit of spike glycoprotein
Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) has posed a great concern in human population. To fight coronavirus emergence, we have dissected the conserved amino acid region of the internal fusion peptide in the S2 subunit of Spike glycoprotein of SARS-CoV-2 to design new inhibitory...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10384657/ https://www.ncbi.nlm.nih.gov/pubmed/37422270 http://dx.doi.org/10.1016/j.virusres.2023.199170 |
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author | Stincarelli, Maria Alfreda Quagliata, Michael Di Santo, Andrea Pacini, Lorenzo Fernandez, Feliciana Real Arvia, Rosaria Rinaldi, Silvia Papini, Anna Maria Rovero, Paolo Giannecchini, Simone |
author_facet | Stincarelli, Maria Alfreda Quagliata, Michael Di Santo, Andrea Pacini, Lorenzo Fernandez, Feliciana Real Arvia, Rosaria Rinaldi, Silvia Papini, Anna Maria Rovero, Paolo Giannecchini, Simone |
author_sort | Stincarelli, Maria Alfreda |
collection | PubMed |
description | Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) has posed a great concern in human population. To fight coronavirus emergence, we have dissected the conserved amino acid region of the internal fusion peptide in the S2 subunit of Spike glycoprotein of SARS-CoV-2 to design new inhibitory peptides. Among the 11 overlapping peptides (9-23-mer), PN19, a 19-mer peptide, exhibited a powerful inhibitory activity against different SARS-CoV-2 clinical isolate variants in absence of cytotoxicity. The PN19 inhibitory activity was found to be dependent on conservation of the central Phe and C-terminal Tyr residues in the peptide sequence. Circular dichroism spectra of the active peptide exhibited an alpha-helix propensity, confirmed by secondary structure prediction analysis. The PN19 inhibitory activity, exerted in the first step of virus infection, was reduced after peptide adsorption treatment with virus-cell substrate during fusion interaction. Additionally, PN19 inhibitory activity was reduced by adding S2 membrane-proximal region derived peptides. PN19 showed binding ability to the S2 membrane proximal region derived peptides, confirmed by molecular modelling, playing a role in the mechanism of action. Collectively, these results confirm that the internal fusion peptide region is a good candidate on which develop peptidomimetic anti SARS-CoV-2 antivirals. |
format | Online Article Text |
id | pubmed-10384657 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-103846572023-07-30 SARS-CoV-2 inhibitory activity of a short peptide derived from internal fusion peptide of S2 subunit of spike glycoprotein Stincarelli, Maria Alfreda Quagliata, Michael Di Santo, Andrea Pacini, Lorenzo Fernandez, Feliciana Real Arvia, Rosaria Rinaldi, Silvia Papini, Anna Maria Rovero, Paolo Giannecchini, Simone Virus Res Article Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) has posed a great concern in human population. To fight coronavirus emergence, we have dissected the conserved amino acid region of the internal fusion peptide in the S2 subunit of Spike glycoprotein of SARS-CoV-2 to design new inhibitory peptides. Among the 11 overlapping peptides (9-23-mer), PN19, a 19-mer peptide, exhibited a powerful inhibitory activity against different SARS-CoV-2 clinical isolate variants in absence of cytotoxicity. The PN19 inhibitory activity was found to be dependent on conservation of the central Phe and C-terminal Tyr residues in the peptide sequence. Circular dichroism spectra of the active peptide exhibited an alpha-helix propensity, confirmed by secondary structure prediction analysis. The PN19 inhibitory activity, exerted in the first step of virus infection, was reduced after peptide adsorption treatment with virus-cell substrate during fusion interaction. Additionally, PN19 inhibitory activity was reduced by adding S2 membrane-proximal region derived peptides. PN19 showed binding ability to the S2 membrane proximal region derived peptides, confirmed by molecular modelling, playing a role in the mechanism of action. Collectively, these results confirm that the internal fusion peptide region is a good candidate on which develop peptidomimetic anti SARS-CoV-2 antivirals. Elsevier 2023-07-15 /pmc/articles/PMC10384657/ /pubmed/37422270 http://dx.doi.org/10.1016/j.virusres.2023.199170 Text en © 2023 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Stincarelli, Maria Alfreda Quagliata, Michael Di Santo, Andrea Pacini, Lorenzo Fernandez, Feliciana Real Arvia, Rosaria Rinaldi, Silvia Papini, Anna Maria Rovero, Paolo Giannecchini, Simone SARS-CoV-2 inhibitory activity of a short peptide derived from internal fusion peptide of S2 subunit of spike glycoprotein |
title | SARS-CoV-2 inhibitory activity of a short peptide derived from internal fusion peptide of S2 subunit of spike glycoprotein |
title_full | SARS-CoV-2 inhibitory activity of a short peptide derived from internal fusion peptide of S2 subunit of spike glycoprotein |
title_fullStr | SARS-CoV-2 inhibitory activity of a short peptide derived from internal fusion peptide of S2 subunit of spike glycoprotein |
title_full_unstemmed | SARS-CoV-2 inhibitory activity of a short peptide derived from internal fusion peptide of S2 subunit of spike glycoprotein |
title_short | SARS-CoV-2 inhibitory activity of a short peptide derived from internal fusion peptide of S2 subunit of spike glycoprotein |
title_sort | sars-cov-2 inhibitory activity of a short peptide derived from internal fusion peptide of s2 subunit of spike glycoprotein |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10384657/ https://www.ncbi.nlm.nih.gov/pubmed/37422270 http://dx.doi.org/10.1016/j.virusres.2023.199170 |
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