Homology modelling and characterization of three-dimensional (3d) protein structures of selected variants of cyp3a4
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Date
2022
Authors
Journal Title
Journal ISSN
Volume Title
Publisher
University of the Western Cape
Abstract
The efficacy and toxicity of several drugs and prodrugs are influenced by the interindividual
genetic variations in drug-metabolising enzymes. Cytochrome P450
enzymes constitute the major metabolising enzymes in humans. Cytochrome 3A4
(CYP3A4) is the highest abundantly expressed human cytochrome P450 enzyme
metabolising about 40% of marketed drugs. Several studies have shown the
significant effects of CYP3A4 single nucleotide variability on its enzymatic activity
and the pharmacokinetic parameters of metabolized drugs. However, there is a
paucity of information on the molecular characteristics (including threedimensional
protein structures, physicochemical properties, and molecular
dynamics characteristics) of single nucleotide variants of CYP3A4 enzymes that
may be correlated with the reported variability of their enzymatic activities.
Description
>Magister Scientiae - MSc
Keywords
Bioinformatics, Pharmacogenomics, Molecular dynamics, Homology, Pharmacy