VIRTUAL MODELING OF INHIBITING THE HELICOBACTER PYLORI ACID RESISTANCE SYSTEM

Background and Aim:One of the most important pathogens in the digestive system is Helicobacter pylori. The catalytic activity of urease enzyme is dependent on nickel. One of the key subunits of urease, which causes the transfer of nickel to an enzyme active site, is UreG. The aim of this study was to investigate the pharmacodynamics properties of compounds on inhibiting UreG proteins and proton pumpMethods:Twenty same combinations of the composition with the 1,3-caffeoylquinic acid plant composition were investigated. the most effective plant compounds have been identified. With the help of the PubChem database, the structure of the compounds was obtained and the ligands were designed with Chemsketch software. The UreG protein crystallographic file and proton pump were obtained by PDB protein database (4HI0, 3ux41) and SPDBV software optimized its energy level. Protein-ligand docking configuration was defined with AutoDock4 software and the algorithm was created with Cygwin software, and finally, the analysis of the information obtained from the files which were reported.Results:The binding energy between this ligand and the substrate 4HI0, would be -7.75Kcal/mol, and this parameter for the interconnection of this compound with the 3UX41 substrate would be -5.99Kcal/mol. The best result which was obtained in this study belongs to the interaction of this ligand with the desired substrates.Conclusion:the plant was introduced as an effective herb in the treatment of Helicobacter pylori infection. For this purpose, extraction of this plant extract and molecular and laboratory dynamical studies can be expanded and completed