Introduction: Millions of people in the world suffer from various types of acute respiratory infectious diseases every year as one of the most important medical problems of today's human societies. Influenza is one of the most important diseases that causes damage to the upper and lower respiratory system. The outbreak of the influenza virus in 1918 infected more than 500 million people worldwide, which was the largest pandemic in the history of this disease and killed more than 20 million people; Also, in 1956 and 1968, other pandemics caused by this deadly virus occurred, which caused the death of more than one million people in the world; And before the outbreak of the Covid-19 disease, which spread all over the world since the end of 2019, it was considered as the biggest threat to human health. The first pandemic outbreak of H1N1 swine flu disease in the 21st century occurred in early April 2008 equivalent to March 2009 in Mexico and caused a large number of people around the world to be infected and caused high mortality and economic damage. It spread all over the world and was known as the swine flu disease early on, and due to the rapid spread of the disease in more than 200 countries, it was named the new H1N1 flu by the World Health Organization that year. Researchers' research has shown that drugs made against hemagglutinin and neuraminidase can improve the complications caused by influenza virus. In recent years, drug resistance has been observed, which is due to the high consumption of drugs; Therefore, it is necessary to introduce a more effective inhibitor to inhibit the neuroaminidase enzyme, which is one of the effective enzymes in the pathogenesis of the swine flu virus.
Methods: In this study, which was carried out by bioinformatics simulation method, the structural file of neuroaminidase protein was downloaded from the NCBI database, and since this protein has 4 identical chains, chain A was selected, and using Gromax software package, energy optimization and minimization steps were performed. It was done. The drugs used in this study were downloaded from the Pubcam database and converted to .pdb format with the OpenBabel software. Molecular docking was done with HEX8.0.0 software and the binding position of each drug on the protein was obtained with Argoslab software; The results were analyzed using WebLab Viewer, Piemol, Excel and Leagueplot software.
Results: The herbal compounds studied in this research were from the flavonol class, including myristin, murine, fistin, quercetin, kaempferol, and galangin, and the antiviral compounds studied included oseltamivir, zanamivir, amantadine, and rimantadine. In this study, it was observed that the antiviral drug rimantadine binds to amino acid proline 431 of the enzyme by hydrogen bonding; Also, myristin, quercetin, and fistin were bound to tryptophan 189 in the active site of neuroaminidase enzyme, and galangin, kaempferol, and murine were all bound to arginine 371 amino acid in the binding pocket of the enzyme.
Conclusion: Arginine 371 is located in the active site of the enzyme;This study showed that galangin, murine and kaempferol from the flavonol class of flavonoids by binding to arginine 371 of the active site of the enzyme inhibit the catalytic function of the enzyme.