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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...

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Autores principales: Syrbu, S. A., Semeikin, A. S., Lebedeva, N. Sh., Gubarev, Yu. A., Yurina, E. S., Guseinov, S. S., Koifman, O. I.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2022
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.
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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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