Novel porphyrin compounds containing benzothiazole, benzoxazole, and benzimidazole moieties have been prepared and their structures have been confi rmed. Molecular docking of non-symmetric hetaryl-substituted porphyrins and chlorin e6 with SARS-CoV-2 helicase has been carried out. The affi nity of hetaryl-substituted porphyrins to this protein has been found signifi cantly higher than that of the drugs approved by the FDA and chlorin e6. The structure of the complexes of SARS-CoV-2 helicase with the considered macroheterocyclic compounds has been analyzed. Possible ways to inhibit and photoinactivate SARS-CoV helicase have been suggested basing on the localization of porphyrins and chlorin e6 in the helicase domains.
A systematic spectral study of the interaction of DNA with a number of tetra-and tricationic porphyrins, in which the N-methyl group is located in the para-or meta-position of the pyridyl substituent, has been carried out. The conditions for the formation of intercalation complexes of DNA with the studied porphyrins were established. It was shown that DNA exhibits greater affinity for porphyrins with an N-methyl group in the para-position of the peripheral substituent, compared to porphyrins with an N-methyl group in the meta-position. Intercalation complexes of DNA with porphyrins with the meta-position of the N-methyl group are characterized by spectral features, such as a slight bathochromic shift of the Soret band in the UV-Visible spectrum and the absence of band inversion in the fluorescence spectrum of intercalated porphyrins. For DNA complexes with monohetaryl-substituted porphyrins, a "semi-intercalation" binding model has been proposed.
The results of experimental studies of the interaction of the S-protein with a monohetaryl-substituted porphyrin containing a benzimidazole residue are presented. It has been revealed that the S-protein forms high-affinity complexes with the specified porphyrin. The porphyrin binding by the SARS-CoV-2 S-protein has proceeded stepwise; at the first stage, the driving force of the complexation is electrostatic interaction between the surface negatively charged regions of the protein and cationic substituents of the porphyrin. At the second stage, the target complex of the S-protein with the porphyrin is formed. It has been established that the introduction of 5-[4′-(N-methyl-1,3-benzimidazol-2-yl)phenyl]-10,15,20-tri-(N-methyl-3′-pyridyl)porphyrin triiodide into a solution of the S-protein complex with the angiotensin-converting enzyme leads to the replacement of the latter with the porphyrin. Displacement of the angiotensin-converting enzyme from the complex with the S-protein under the action of 5-[4′-(N-methyl-1,3-benzimidazol-2-yl)phenyl]-10,15,20-tri-(N-methyl-3′-pyridyl)porphyrin triiodide is the experimental evidence for the porphyrin binding at the receptor-binding domain of the S-protein.
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