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• W2077896325 endingPage "8011" @default.
• W2077896325 startingPage "8000" @default.
• W2077896325 abstract "CYP2C9 is a significant P450 protein responsible for drug metabolism. With the increased use of heterocyclic compounds in drug design, a rapid and efficient predrug screening of these potential type II binding compounds is essential to avoid adverse drug reactions. To understand binding modes, we use quinoline-4-carboxamide analogues to study the factors that determine the structure-activity relationships. The results of this study suggest that the more accessible pyridine with the nitrogen para to the linkage can coordinate directly with the ferric heme iron, but this is not seen for the meta or ortho isomers. The pi-cation interaction of the naphthalene moiety and Arg 108 residue may also assist in stabilizing substrate binding within the active-site cavity. The type II substrate binding affinity is determined by the combination of steric, electrostatic, and hydrophobicity factors; meanwhile, it is enhanced by the strength of lone pair electrons coordination with the heme iron." @default.
• W2077896325 created "2016-06-24" @default.
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• W2077896325 date "2008-11-19" @default.
• W2077896325 modified "2023-09-26" @default.
• W2077896325 title "Cytochrome P450 2C9 Type II Binding Studies on Quinoline-4-Carboxamide Analogues" @default.
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• W2077896325 doi "https://doi.org/10.1021/jm8011257" @default.
• W2077896325 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2630467" @default.
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• W2077896325 hasPublicationYear "2008" @default.
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