In silico Design of some novel perfusion RSV F glycoprotein inhibitors

Respiratory syncytial virus (RSV) is a leading cause of pneumonia and bronchiolitis in young children and the elderly. Therapeutic small molecules have been developed that bind the RSV F glycoprotein and inhibit membrane fusion, yet their binding sites and molecular mechanisms of action remain largely unknown. Considering the topological description of RSV F glycoprotein and the 2D pose view of the primary ligand 5NK, (2-[[2-[[1-(2-azanylethyl) piperidin-4-yl] amino]-4-methyl-benzimidazol-1-yl] methyl]-6-methyl-pyridin-3-ol) of the target, few of its analogs (ps1-ps8) were made for the purpose of molecular docking. After performing the individual docking study it has been observed that the test compound ‘ps1’ with its 33rd conformer lying closest to the complementary residue (GLU487), i.e.; 9.28 Å, whereas the distance observed between the co-crystal and GLU 487 was 7.13 Å. The other compounds in the test series also met the satisfactory criteria. The initial study set the momentum for further exploration and subsequently development of a novel agent, may become a lethal weapon for RSV.