Реферат: Viral surface proteins play a key role in the life cycle of viruses, ensuring the fusion of the viral envelope and the cell membrane. Conformational rearrangements of proteins lead to the unification of the lipid bilayers of the cell membrane and the viral envelope and the formation of a fusion pore through which the viral genome penetrates into the cytoplasm of the cell. On the basis of structural similarity, viral fusion proteins are divided into three main classes. Here, structural features of type I fusion proteins are considered, such as influenza virus haemagglutinin (HA) and the spike protein of SARS-CoV-2 (Figure 1). Proteins are homotrimeric formations consisting of three identical subunits. They contain α-helical structures and a fusion peptide located closer to the N-terminus and hidden in the middle of the protein trimer. The fusion mechanisms of these proteins are similar and are mediated by heptad repeats (HR). Pharmacophore profile of potential binding sites of HA and S-protein inhibitors were considered using molecular modelling methods. The described binding sites have a similar pharmacophore profile. Perhaps this explains the antiviral activity of umifenovir and borneol esters against the influenza virus and the S-protein of the coronavirus. According to the results of theoretical calculations in combination with the biological experiments data [1-3], these compounds bind into HA and S-protein, inhibiting protein conformational rearrangements. Perhaps this fact may be a loophole for the search and development of broad-spectrum antiviral drugs.

Библиографическая ссылка: Borisevich S.S.
Search for Inhibitors of Surface Viral Proteins I Type by Molecular Modeling
XXIX Symposium on Bioinformatics and computer-aided drug discovery 18-20 Sep 2023