Introduction: Acute respiratory infectious diseases are one of the most important medical problems of societies, and swine flu, which causes damage to the upper and lower respiratory system, is one of the most important types of these diseases. Influenza virus usually infects a large group of people in two ways, seasonal and pandemic. The outbreak of seasonal diseases with the beginning of the winter season causes more high-risk groups such as children and the elderly to become infected, and in a pandemic, about 25% of the world's population is affected, and it affects all age groups and causes a high number of deaths. At the same time as influenza occurs, other complications may also occur in the patient's body, which can prolong the course of the disease or, in some cases, lead to death; One of the most important complications is primary viral pneumonia, which in most cases causes secondary bacterial pneumonia. The neuroaminidase enzyme of the H1N1 influenza virus breaks down the terminal sialic acid of the glycoconjugates on the surface of the target cells in the upper respiratory tract of mammals. Research has shown that drugs that are made against hemagglutinin and neuraminidase can improve the symptoms of influenza. The drug resistance observed against the treatment has caused the need to introduce alternative and more effective inhibitory treatments.
Methods: In this study, which was carried out in a computer environment and by bioinformatics method, the neuroaminidase enzyme crystallography file was received from the NCBI database, and after selecting the A chain, it was optimized and reduced with Gromax software. The file with the extension .sdf of the compounds used in this research was downloaded from the Pubcam database and converted to .pdb format with the OpenBabel software. Molecular docking was done in the HEX8.0.0 software environment and the binding position of the studied compounds on the protein was obtained using Argoslab software. The analysis of the obtained results was done with WebLab Viewer, Piemol, Excel and Leagueplot software.
Results: The researched compounds from the flavonol class include myristin, murine, fistin, quercetin, kaempferol and galangin and from the flavon class including disometin, luteolin, apigenin, chrysin, catechin, hesperitin, genistein, nobiltin, naringin and hispidolin and the studied antiviral compounds include were oseltamivir, zanamivir, amantadine and rimantadine.
From this study, it was found that the antiviral drug rimantadine binds to amino acid proline 431 of the enzyme by hydrogen bonding; Also, myristin, quercetin and fistin from the flavonol class were bound to tryptophan 189 and galangin, kaempferol and murine all three were bound to the amino acid arginine 371 in the binding pocket of the enzyme.
Conclusion: It was also observed that chrysin, genistein, hesperitin, naringin and luteolin from the flavone class were bound to the amino acid arginine 371 of the active site of the enzyme, and catechin, hispidolin and nobiltin were bound to three different sites in the binding site of the enzyme.he results of this study showed that the three flavonoid compounds galangin, murine, and kaempferol from the flavonol class and chrysin, genistein, hesperitin, naringin, and luteolin from the flavone class flavonoids, by binding to arginine 371 of the enzyme's active site, inhibit the enzyme's function; From this study, it was found that naringin is a stronger inhibitor due to its greater affinity for the active site of the enzyme.