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...

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Veröffentlicht in:Russian chemical bulletin 2022, Vol.71 (11), p.2495-2504
Hauptverfasser: Syrbu, S. A., Semeikin, A. S., Lebedeva, N. Sh, Gubarev, Yu. A., Yurina, E. S., Guseinov, S. S., Koifman, O. I.
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Sprache:eng
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Zusammenfassung: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.
ISSN:1066-5285
1573-9171
DOI:10.1007/s11172-022-3679-8