We compared the electrostatic properties of the spike proteins (S-proteins) of three coronaviruses, SARS-CoV, MERS-CoV, and SARS-CoV-2, and their interactions with photosensitizers (PSs), octacationic octakis(cholinyl)zinc phthalocyanine (Zn-PcChol 8+ ) and monocationic methylene blue (MB). We found a major common PS binding site at the connection of the S-protein stalk and head. The molecules of Zn-PcChol 8+ and MB also form electrostatic encounter complexes with large area of negative electrostatic potential at the head of the S-protein of SARS-CoV-2, between fusion protein and heptad repeat 1 domain. The top of the SARS-CoV spike head demonstrates a notable area of electrostatic contacts with Zn-PcChol 8+ and MB that corresponds to the N-terminal domain. The S-protein protomers of SARS-CoV-2 in “open” and “closed” conformations demonstrate different ability to attract PS molecules. In contrast with Zn-PcChol 8+ , MB possesses the ability to penetrate inside the pocket formed as a result of SARS-CoV-2 receptor binding domain transition into the “open” state. The existence of binding site for cationic PSs common to the S-proteins of SARS-CoV, SARS-CoV-2, and MERS-CoV creates prospects for the wide use of this type of PSs to combat the spread of coronaviruses.
【저자키워드】 SARS-CoV-2, SARS-CoV, MERS-CoV, Spike protein, Methylene blue, Brownian dynamics, photosensitizer, octakis(cholinyl)zinc phthalocyanine, 【초록키워드】 Coronaviruses, SARS-CoV-2 receptor, binding site, Spread, fusion protein, N-terminal domain, Interaction, S-protein, Contact, connection, domain, conformation, binding domain, heptad repeat, the spike protein, complexes, notable, electrostatic, cationic, penetrate, 【제목키워드】 spike, Dynamics, bind, Site,