Theoretical quantitative structure–activity relationships of flavone ligands interacting with cytochrome P450 1A1 and 1A2 isozymes

[Display omitted] Theoretical descriptors obtained from quantum mechanical calculations on isolated ligands in different media and molecular dynamics simulations of ligand–enzyme complexes have been used to obtain a quantitative rationalization of the inhibition of CYP1A2 and CYP1A2 by three series...

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Published inBioorganic & medicinal chemistry Vol. 13; no. 14; pp. 4366 - 4374
Main Authors Iori, F., Fonseca, R. da, Ramos, M. João, Menziani, M.C.
Format Journal Article
LanguageEnglish
Published Oxford Elsevier Ltd 15.07.2005
Elsevier Science
Subjects
Binding Sites
Biological and medical sciences
Cytochrome P-450 CYP1A1 - metabolism
Cytochrome P-450 CYP1A2 - metabolism
Flavones - metabolism
Humans
Ligands
Medical sciences
Miscellaneous
Models, Molecular
Pharmacology. Drug treatments
Structure-Activity Relationship
Unspecific monooxygenase
Enzyme
Isozyme
Ligand
Cytochrome P450
Molecular dynamics method
Prediction
Theoretical study
Inhibitor enzyme complex
Binding site
Selectivity
Flavonoid
Modeling
Flavanone derivatives
Structure activity relation
Molecular model
Flavone derivatives
Drug-metabolizing enzyme
Oxidoreductases
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Summary:[Display omitted] Theoretical descriptors obtained from quantum mechanical calculations on isolated ligands in different media and molecular dynamics simulations of ligand–enzyme complexes have been used to obtain a quantitative rationalization of the inhibition of CYP1A2 and CYP1A2 by three series of flavonoids. Predictive models obtained through one-descriptor QSAR studies and mechanistic explanations have been obtained for recognition and selectivity.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0968-0896
1464-3391
DOI:10.1016/j.bmc.2005.04.066