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Synthesis of water-soluble porphyrin with tyrosine fragments and study of its interaction with S-protein of SARS-CoV-2
The multistage purposeful synthesis of 5,15-bis(4′-l-N-tyrosinylamidophenyl)-10,20-bis(N-methylpyridin-3′-yl)porphine diiodide was carried out, and the optimum synthesis conditions were determined. 5,15-Bis(4′-nitrophenyl)-10,20-bis(pyridin-3′-yl)porphine served as the starting porphyrin. The struct...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer US
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9762635/ https://www.ncbi.nlm.nih.gov/pubmed/36569660 http://dx.doi.org/10.1007/s11172-022-3679-8 |
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author | Syrbu, S. A. Semeikin, A. S. Lebedeva, N. Sh. Gubarev, Yu. A. Yurina, E. S. Guseinov, S. S. Koifman, O. I. |
author_facet | Syrbu, S. A. Semeikin, A. S. Lebedeva, N. Sh. Gubarev, Yu. A. Yurina, E. S. Guseinov, S. S. Koifman, O. I. |
author_sort | Syrbu, S. A. |
collection | PubMed |
description | The multistage purposeful synthesis of 5,15-bis(4′-l-N-tyrosinylamidophenyl)-10,20-bis(N-methylpyridin-3′-yl)porphine diiodide was carried out, and the optimum synthesis conditions were determined. 5,15-Bis(4′-nitrophenyl)-10,20-bis(pyridin-3′-yl)porphine served as the starting porphyrin. The structure, individual character, and purity of the target compound were proved by electron spectroscopy, (1)H NMR spectroscopy, mass spectrometry (MALDI TOF), and TLC. Specific features of the interaction of the synthesized porphyrin with S-protein of SARS-CoV-2 were studied using spectral and thermochemical methods, including conditions of photoirradiation. The photoirradiation of the synthesized porphyrin in a complex with the SARS-CoV-2 S-protein can result in the partial oxidation of amino acid residues of the protein and distort its primary and secondary structures. The photoirradiation of the S-protein complex with the porphyrin decreases its thermal resistance to melting by 15 °C compared to the free S-protein and causes porphyrin release. |
format | Online Article Text |
id | pubmed-9762635 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Springer US |
record_format | MEDLINE/PubMed |
spelling | pubmed-97626352022-12-20 Synthesis of water-soluble porphyrin with tyrosine fragments and study of its interaction with S-protein of SARS-CoV-2 Syrbu, S. A. Semeikin, A. S. Lebedeva, N. Sh. Gubarev, Yu. A. Yurina, E. S. Guseinov, S. S. Koifman, O. I. Russ Chem Bull Full Articles The multistage purposeful synthesis of 5,15-bis(4′-l-N-tyrosinylamidophenyl)-10,20-bis(N-methylpyridin-3′-yl)porphine diiodide was carried out, and the optimum synthesis conditions were determined. 5,15-Bis(4′-nitrophenyl)-10,20-bis(pyridin-3′-yl)porphine served as the starting porphyrin. The structure, individual character, and purity of the target compound were proved by electron spectroscopy, (1)H NMR spectroscopy, mass spectrometry (MALDI TOF), and TLC. Specific features of the interaction of the synthesized porphyrin with S-protein of SARS-CoV-2 were studied using spectral and thermochemical methods, including conditions of photoirradiation. The photoirradiation of the synthesized porphyrin in a complex with the SARS-CoV-2 S-protein can result in the partial oxidation of amino acid residues of the protein and distort its primary and secondary structures. The photoirradiation of the S-protein complex with the porphyrin decreases its thermal resistance to melting by 15 °C compared to the free S-protein and causes porphyrin release. Springer US 2022-12-19 2022 /pmc/articles/PMC9762635/ /pubmed/36569660 http://dx.doi.org/10.1007/s11172-022-3679-8 Text en © Springer Science+Business Media LLC 2022 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
spellingShingle | Full Articles Syrbu, S. A. Semeikin, A. S. Lebedeva, N. Sh. Gubarev, Yu. A. Yurina, E. S. Guseinov, S. S. Koifman, O. I. Synthesis of water-soluble porphyrin with tyrosine fragments and study of its interaction with S-protein of SARS-CoV-2 |
title | Synthesis of water-soluble porphyrin with tyrosine fragments and study of its interaction with S-protein of SARS-CoV-2 |
title_full | Synthesis of water-soluble porphyrin with tyrosine fragments and study of its interaction with S-protein of SARS-CoV-2 |
title_fullStr | Synthesis of water-soluble porphyrin with tyrosine fragments and study of its interaction with S-protein of SARS-CoV-2 |
title_full_unstemmed | Synthesis of water-soluble porphyrin with tyrosine fragments and study of its interaction with S-protein of SARS-CoV-2 |
title_short | Synthesis of water-soluble porphyrin with tyrosine fragments and study of its interaction with S-protein of SARS-CoV-2 |
title_sort | synthesis of water-soluble porphyrin with tyrosine fragments and study of its interaction with s-protein of sars-cov-2 |
topic | Full Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9762635/ https://www.ncbi.nlm.nih.gov/pubmed/36569660 http://dx.doi.org/10.1007/s11172-022-3679-8 |
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