title: Study on molecular mechanism and 3D-QSAR of influenza neuraminidase inhibitors.
abstract: Neuraminidase (NA) is a critical enzyme of the influenza virus and many inhibitors targeting to this enzyme are quite efficient and encouraging as anti-influenza agents. In this paper the binding model of five series of inhibitors to NA was examined using molecular simulation method. The resulted conformation and orientation of the compounds were directly put into CoMSIA study. The most significant amino acid residues at binding sites and the requirement for features of substituents were applied to direct design of new inhibitors. The robust QSAR model and its three-dimensional contour map provided guidelines to building novel compounds with new scaffold and for structural optimization of current molecules.
authors.affiliation: Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100050, China.
authors.forename: Xiang
authors.initials: X
authors.lastname: Yi
authors.forename: Zongru
authors.initials: Z
authors.lastname: Guo
authors.forename: Feng Ming
authors.initials: FM
authors.lastname: Chu
mesh_terms: D000465:Algorithms; D001665:Binding Sites; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D008958:Models, Molecular; D009439:Neuraminidase / Q000037:antagonists & inhibitors* / Q000737:chemistry; D009975:Orthomyxoviridae / Q000201:enzymology*; D011487:Protein Conformation; D021281:Quantitative Structure-Activity Relationship
chemical_list: D004791:Enzyme Inhibitors; D009439:Neuraminidase