Publication Cover
Xenobiotica
the fate of foreign compounds in biological systems
Volume 48, 2018 - Issue 12
368
Views
7
CrossRef citations to date
0
Altmetric
General Xenobiochemistry

Allosteric activation of cytochrome P450 3A4 by efavirenz facilitates midazolam binding

, , , , , , , , & show all
Pages 1227-1236 | Received 07 Oct 2017, Accepted 29 Nov 2017, Published online: 18 Dec 2017

References

  • Atkins WM. (2005). Non-Michaelis-Menten kinetics in cytochrome P450-catalyzed reactions. Annu Rev Pharmacol Toxicol 45:291–310
  • Attia TZ, Yamashita T, Miyamoto M, et al. (2012). Comparison of cytochrome p450 mediated metabolism of three central nervous system acting drugs. Chem Pharm Bull (Tokyo) 60:1544–9
  • Basran J, Rafice SA, Chauhan N, et al. (2008). A kinetic, spectroscopic, and redox study of human tryptophan 2,3-dioxygenase. Biochemistry 47:4752–60
  • Berendsen HJC, Postma JPM, van Gunsteren WF, et al. (1984). Molecular-dynamics with coupling to an external bath. J Chem Phys 81:3684–90
  • Blobaum AL, Bridges TM, Byers FW, et al. (2013). Heterotropic activation of the midazolam hydroxylase activity of CYP3A by a positive allosteric modulator of mGlu5: in vitro to in vivo translation and potential impact on clinically relevant drug-drug interactions. Drug Metab Dispos 41:2066–75
  • Chen H, Chen W, Gan LS, Mutlib AE. (2003). Metabolism of (S)-5,6-difluoro-4-cyclopropylethynyl-4-trifluoromethyl-3, 4-dihydro-2(1H)-quinazolinone, a non-nucleoside reverse transcriptase inhibitor, in human liver microsomes. Metabolic activation and enzyme kinetics. Drug Metab Dispos 31:122–32
  • Domanski TL, He YA, Khan KK, et al. (2001). Phenylalanine and tryptophan scanning mutagenesis of CYP3A4 substrate recognition site residues and effect on substrate oxidation and cooperativity. Biochemistry 40:10150–60
  • Duan Y, Wu C, Chowdhury S, et al. (2003). A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations. J Comput Chem 24:1999–2012
  • Ekins S, Ring BJ, Binkley SN, et al. (1998a). Autoactivation and activation of the cytochrome P450s. Int J Clin Pharmacol Ther 36:642–51
  • Ekins S, Vandenbranden M, Ring BJ, et al. (1998b). Further characterization of the expression in liver and catalytic activity of CYP2B6. J Pharmacol Exp Ther 286:1253–9
  • Ekroos M, Sjogren T. (2006). Structural basis for ligand promiscuity in cytochrome P450 3A4. Proc Natl Acad Sci USA 103:13682–7
  • Essmann U, Perera L, Berkowitz ML, et al. (1995). A smooth particle Mesh Ewald method. J Chem Phys 103:8577–93
  • Famiglini V, Silvestri R. (2016). Focus on chirality of HIV-1 non-nucleoside reverse transcriptase inhibitors. Molecules 21:E221
  • Hendrychova T, Anzenbacherova E, Hudecek J, et al. (2011). Flexibility of human cytochrome P450 enzymes: molecular dynamics and spectroscopy reveal important function-related variations. Biochim Biophys Acta 1814:58–68
  • Henshall J, Galetin A, Harrison A, Houston JB. (2008). Comparative analysis of CYP3A heteroactivation by steroid hormones and flavonoids in different in vitro systems and potential in vivo implications. Drug Metab Dispos 36:1332–40
  • Hess B, Bekker H, Berendsen HJC, Fraaije JGEM. (1997). LINCS: a linear constraint solver for molecular simulations. J Comput Chem 18:1463–72
  • Hodgson J. (2001). ADMET-turning chemicals into drugs. Nat Biotechnol 19:722–6
  • Hoover WG. (1985). Canonical dynamics: equilibrium phase-space distributions. Phys Rev A 31:1695–7
  • Hosea NA, Miller GP, Guengerich FP. (2000). Elucidation of distinct ligand binding sites for cytochrome P450 3A4. Biochemistry 39:5929–39
  • Hummel MA, Gannett PM, Aguilar JS, Tracy TS. (2004). Effector-mediated alteration of substrate orientation in cytochrome P450 2C9. Biochemistry 43:7207–14
  • Hutzler JM, Tracy TS. (2002). Atypical kinetic profiles in drug metabolism reactions. Drug Metab Dispos 30:355–62
  • Isin EM, Guengerich FP. (2006). Kinetics and thermodynamics of ligand binding by cytochrome P450 3A4. J Biol Chem 281:9127–36
  • Jorgensen WL, Chandrasekhar J, Madura JD, et al. (1983). Comparison of simple potential functions for simulating liquid water. J Chem Phys 79:926
  • Keubler A, Weiss J, Haefeli WE, et al. (2012). Drug interaction of efavirenz and midazolam: efavirenz activates the CYP3A-mediated midazolam 1'-hydroxylation in vitro. Drug Metab Dispos 40:1178–82
  • Korzekwa KR, Krishnamachary N, Shou M, et al. (1998). Evaluation of atypical cytochrome P450 kinetics with two-substrate models: evidence that multiple substrates can simultaneously bind to cytochrome P450 active sites. Biochemistry 37:4137–47
  • Kosugi Y, Takahashi J. (2015). Species differences and substrate specificity of CYP3A heteroactivation by efavirenz. Xenobiotica 45:345–52
  • Lin JH, Lu AY. (1998). Inhibition and induction of cytochrome P450 and the clinical implications. Clin Pharmacokinet 35:361–90
  • Marohnic CC, Panda SP, Martasek P, Masters BS. (2006). Diminished FAD binding in the Y459H and V492E Antley-Bixler syndrome mutants of human cytochrome P450 reductase. J Biol Chem 281:35975–82
  • Mikus G, Heinrich T, Bodigheimer J, et al. (2017). Semisimultaneous midazolam administration to evaluate the time course of CYP3A activation by a single oral dose of efavirenz. J Clin Pharmacol 57:899–905
  • Miyamoto M, Yamashita T, Yasuhara Y, et al. (2015). Membrane anchor of cytochrome P450 reductase suppresses the uncoupling of cytochrome P450. Chem Pharm Bull (Tokyo) 63:286–94
  • Miyamoto S, Kollman PA. (1992). SETTLE: an analytical version of the SHAKE and RATTLE algorithm for rigid water models. J Comput Chem 13:952–62
  • Monteiro LM, Lione VF, do Carmo FA, et al. (2012). Development and characterization of a new oral dapsone nanoemulsion system: permeability and in silico bioavailability studies. Int J Nanomedicine 7:5175–82
  • Nath A, Grinkova YV, Sligar SG, Atkins WM. (2007). Ligand binding to cytochrome P450 3A4 in phospholipid bilayer nanodiscs: the effect of model membranes. J Biol Chem 282:28309–20
  • Ngui JS, Chen Q, Shou M, et al. (2001). In vitro stimulation of warfarin metabolism by quinidine: increases in the formation of 4'- and 10-hydroxywarfarin. Drug Metab Dispos 29:877–86
  • Niwa T, Murayama N, Emoto C, Yamazaki H. (2008). Comparison of kinetic parameters for drug oxidation rates and substrate inhibition potential mediated by cytochrome P450 3A4 and 3A5. Curr Drug Metab 9:20–33
  • Nose S. (1984). A unified formulation of the constant temperature molecular-dynamics methods. J Chem Phys 81:511–19
  • Parrinello M, Rahman A. (1980). Crystal structure and pair potentials: a molecular-dynamics study. Phys Rev Lett 45:1196
  • Pelkonen O, Maenpaa J, Taavitsainen P, et al. (1998). Inhibition and induction of human cytochrome P450 (CYP) enzymes. Xenobiotica 28:1203–53
  • Pronk S, Pall S, Schulz R, et al. (2013). GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit. Bioinformatics (Oxford, England) 29:845–54
  • Roberts AG, Atkins WM. (2007). Energetics of heterotropic cooperativity between alpha-naphthoflavone and testosterone binding to CYP3A4. Arch Biochem Biophys 463:89–101
  • Roberts AG, Campbell AP, Atkins WM. (2005). The thermodynamic landscape of testosterone binding to cytochrome P450 3A4: ligand binding and spin state equilibria. Biochemistry 44:1353–66
  • Sali A, Blundell TL. (1993). Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234:779–815
  • Sevrioukova IF, Poulos TL. (2012). Structural and mechanistic insights into the interaction of cytochrome P4503A4 with bromoergocryptine, a type I ligand. J Biol Chem 287:3510–17
  • Sevrioukova IF, Poulos TL. (2017). Structural basis for regiospecific midazolam oxidation by human cytochrome P450 3A4. Proc Natl Acad Sci USA 114:486–91
  • Shimada T, El-Bayoumy K, Upadhyaya P, et al. (1997). Inhibition of human cytochrome P450-catalyzed oxidations of xenobiotics and procarcinogens by synthetic organoselenium compounds. Cancer Res 57:4757–64
  • Shou M, Grogan J, Mancewicz JA, et al. (1994). Activation of CYP3A4: evidence for the simultaneous binding of two substrates in a cytochrome P450 active site. Biochemistry 33:6450–5
  • Taavitsainen P, Juvonen R, Pelkonen O. (2001). In vitro inhibition of cytochrome P450 enzymes in human liver microsomes by a potent CYP2A6 inhibitor, trans-2-phenylcyclopropylamine (tranylcypromine), and its nonamine analog, cyclopropylbenzene. Drug Metab Dispos 29:217–22
  • Tang W, Stearns RA. (2001). Heterotropic cooperativity of cytochrome P450 3A4 and potential drug-drug interactions. Curr Drug Metab 2:185–98
  • Tsalkova TN, Davydova NY, Halpert JR, Davydov DR. (2007). Mechanism of interactions of alpha-naphthoflavone with cytochrome P450 3A4 explored with an engineered enzyme bearing a fluorescent probe. Biochemistry 46:106–19
  • Ueng YF, Kuwabara T, Chun YJ, Guengerich FP. (1997). Cooperativity in oxidations catalyzed by cytochrome P450 3A4. Biochemistry 36:370–81
  • von Moltke LL, Greenblatt DJ, Granda BW, et al. (2001). Inhibition of human cytochrome P450 isoforms by nonnucleoside reverse transcriptase inhibitors. J Clin Pharmacol 41:85–91
  • Vrouenraets SM, Wit FW, van Tongeren J, Lange JM. (2007). Efavirenz: a review. Expert Opin Pharmacother 8:851–71
  • Wang RW, Newton DJ, Liu N, et al. (2000). Human cytochrome P-450 3A4: in vitro drug-drug interaction patterns are substrate-dependent. Drug Metab Dispos 28:360–6
  • Ward BA, Gorski JC, Jones DR, et al. (2003). The cytochrome P450 2B6 (CYP2B6) is the main catalyst of efavirenz primary and secondary metabolism: implication for HIV/AIDS therapy and utility of efavirenz as a substrate marker of CYP2B6 catalytic activity. J Pharmacol Exp Ther 306:287–300
  • Williams PA, Cosme J, Vinkovic DM, et al. (2004). Crystal structures of human cytochrome P450 3A4 bound to metyrapone and progesterone. Science 305:683–6
  • Yano JK, Wester MR, Schoch GA, et al. (2004). The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-A resolution. J Biol Chem 279:38091–4
  • Yasukochi Y, Masters BS. (1976). Some properties of a detergent-solubilized NADPH-cytochrome c(cytochrome P-450) reductase purified by biospecific affinity chromatography. J Biol Chem 251:5337–44
  • Zanger UM, Schwab M. (2013). Cytochrome P450 enzymes in drug metabolism: regulation of gene expression, enzyme activities, and impact of genetic variation. Pharmacol Ther 138:103–41

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.