Insights on cytochrome p450 enzymes and inhibitors obtained through QSAR studies.

Citation data:

Molecules (Basel, Switzerland), ISSN: 1420-3049, Vol: 17, Issue: 8, Page: 9283-305

Publication Year:
2012
Usage 81
Abstract Views 44
Full Text Views 35
Link-outs 2
Captures 60
Readers 55
Exports-Saves 5
Social Media 1
Shares, Likes & Comments 1
Citations 31
Citation Indexes 31
Repository URL:
https://digitalcommons.xula.edu/fac_pub/23
PMID:
22864238
DOI:
10.3390/molecules17089283
PMCID:
PMC3666846
Author(s):
Sridhar, Jayalakshmi; Liu, Jiawang; Foroozesh, Maryam; Stevens, Cheryl Stevens L. Klein
Publisher(s):
MDPI AG
Tags:
Chemistry; Medicine; 3D-QSAR; SAR; binding/active site; CoMFA; pharmacophore; Medicinal-Pharmaceutical Chemistry
review description
The cytochrome P450 (CYP) superfamily of heme enzymes play an important role in the metabolism of a large number of endogenous and exogenous compounds, including most of the drugs currently on the market. Inhibitors of CYP enzymes have important roles in the treatment of several disease conditions such as numerous cancers and fungal infections in addition to their critical role in drug-drug interactions. Structure activity relationships (SAR), and three-dimensional quantitative structure activity relationships (3D-QSAR) represent important tools in understanding the interactions of the inhibitors with the active sites of the CYP enzymes. A comprehensive account of the QSAR studies on the major human CYPs 1A1, 1A2, 1B1, 2A6, 2B6, 2C9, 2C19, 2D6, 2E1, 3A4 and a few other CYPs are detailed in this review which will provide us with an insight into the individual/common characteristics of the active sites of these enzymes and the enzyme-inhibitor interactions.