AFM study of the interaction of cytochrome P450 2C9 with phospholipid bilayers

Chemistry and Physics of Lipids
Matthew R NussioJoseph G Shapter

Abstract

Cytochromes P450 (CYP) are key enzymes involved in the metabolism of drugs and other lipophilic xenobiotics and endogenous compounds. In this study, atomic force microscopy was applied to characterise the association of CYP2C9 to dimyristoylphosphatidylcholine (DMPC) supported phospholipid bilayers. CYP2C9 was found to exclusively localise in the gel domains of partially melted DMPC bilayers. Despite lacking the N-terminus transmembrane spanning domain, the CYP2C9 protein appeared to partially embed into the membrane bilayer, as evidenced by an increase in melting temperature of surrounding phospholipids. Reversible binding of CYP2C9 via an engineered His tag to a phospholipid bilayer was facilitated using nickel-chelating lipids, presenting potential applications for biosensor technologies.

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Citations

Sep 13, 2012·Analytical and Bioanalytical Chemistry·Sandrine MorandatKarim El Kirat
Aug 20, 2011·PLoS Computational Biology·Vlad CojocaruRebecca C Wade
Jul 13, 2011·The Journal of Physical Chemistry. a·Karel BerkaMichal Otyepka
Aug 31, 2013·The Journal of Physical Chemistry. B·Karel BerkaMichal Otyepka
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Sep 7, 2019·International Journal of Molecular Sciences·Ghulam MustafaRebecca C Wade
Nov 25, 2020·Chembiochem : a European Journal of Chemical Biology·Chun-Chi ChenRey-Ting Guo

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