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Docking and 3D‐QSAR investigations of pyrrolidine derivatives as potent neuraminidase inhibitors
Author(s) -
Sun Jiaying,
Mei Hu
Publication year - 2012
Publication title -
chemical biology and drug design
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.59
H-Index - 77
eISSN - 1747-0285
pISSN - 1747-0277
DOI - 10.1111/j.1747-0285.2012.01330.x
Subject(s) - pyrrolidine , quantitative structure–activity relationship , chemistry , docking (animal) , neuraminidase , hydrogen bond , stereochemistry , enzyme , molecule , biochemistry , organic chemistry , medicine , nursing
Docking studies of pyrrolidine derivatives indicated that Trp178, Arg371, and Tyr406 were the key residues in the active pocket of influenza neuraminidase (NA). Hydrogen bond and electrostatic factors mainly influenced interactions between pyrrolidine derivatives and NA. Moreover, there was a significant correlation between binding affinity (total scores) and the experimental pIC 50 . Meanwhile, 3D‐QSAR models of 87 pyrrolidine derivatives were developed to understand chemical–biological interactions governing their activities toward NA. Furthermore, R 2 , Q 2 , , and of the models were from 0.731 to 0.830, from 0.560 to 0.611, from 0.762 to 0.875, and from 0.649 to 0.856, respectively. QSAR modeling results elucidated that hydrogen bonds and electrostatic factors highly contributed to inhibitory activity, which was unanimous in the docking results.