Study On The Salt Formation Of Poorly Soluble Compounds And Their Interaction With Key Enzyme Targets Of Plant Viruses

Southern rice black-streaked dwarf virus S9-1 is predicted to encode viral matrix proteins.Viral matrix proteins are the key to viral replication.Therefore,we study the interaction and binding mode of antiviral activity small molecule with SRBSDV P9-1,which can lay a foundation for the development of new and highly effective antiviral drugs.In this study,South rice black-streaked dwarf virus(SRBSDV)P9-1 was obtained as a target protein by prokaryotic expression,and 33 antiviral drugs were obtained by microcalorimetry and isothermal titration calorimetry.The small active molecules were screened for salt formation,and the compounds with different MST and ITC results were salted,and the binding sites of the antiviral activity small molecule and SRBSDV P9-1 were calculated by computer molecule docking.The wild-type SRBSDV P9-1 plasmid was mutated,and the mutant SRBSDV P9-1 was obtained by prokaryotic expression.Finally,the binding force between the drug and the protein was verified by microcalorimetry and isothermal titration calorimetry.The experimental results showed that the mutant plasmid was successfully obtained by site-directed mutagenesis PCR.The results of three methods showed that the arginine 7,arginine 110 and arginine 327 of P9-1 were mutated,and they were small molecules.The binding ability of X2 and X7 is weaker than that of wild type and X2 and X7.The experimental results are consistent with the computer simulation results,indicating that the arginine at positions 7,110 and 327 of SRBSDV P9-1 is the key binding site of X2 and X7.Point;and verify the role of X2 in vivo by Agrobacterium-mediated method.