Homology modelling and characterization of three-dimensional (3d) protein structures of selected variants of cyp3a4

dc.contributor.advisorEgieyeh, Samuel
dc.contributor.authorOmotoso, Christianah Taye
dc.date.accessioned2023-02-02T09:06:27Z
dc.date.accessioned2024-10-29T13:17:58Z
dc.date.available2024-10-29T13:17:58Z
dc.date.issued2022
dc.description>Magister Scientiae - MScen_US
dc.description.abstractThe 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.en_US
dc.description.embargo2024
dc.identifier.urihttps://hdl.handle.net/10566/16345
dc.language.isoenen_US
dc.publisherUniversity of the Western Capeen_US
dc.rights.holderUniversity of the Western Capeen_US
dc.subjectBioinformaticsen_US
dc.subjectPharmacogenomicsen_US
dc.subjectMolecular dynamicsen_US
dc.subjectHomologyen_US
dc.subjectPharmacyen_US
dc.titleHomology modelling and characterization of three-dimensional (3d) protein structures of selected variants of cyp3a4en_US

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