School of Chemistry, Physics and Earth Sciences, Flinders University, Sturt Road, Bedford Park, Adelaide, SA 5001, Australia.
Chem Phys Lipids. 2010 Feb;163(2):182-9. doi: 10.1016/j.chemphyslip.2009.11.003. Epub 2009 Nov 17.
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.
细胞色素 P450（CYP）是参与药物和其他亲脂性异生物及内源性化合物代谢的关键酶。在这项研究中，原子力显微镜被应用于表征细胞色素 P4502C9 与二肉豆蔻酰磷脂酰胆碱（DMPC）支持的磷脂双层的结合。发现细胞色素 P4502C9 仅定位于部分融化的 DMPC 双层的凝胶域中。尽管缺乏 N 端跨膜结构域，细胞色素 P4502C9 蛋白似乎部分嵌入到膜双层中，这可以通过周围磷脂的熔点升高来证明。通过使用镍螯合脂质，通过工程化的 His 标签实现细胞色素 P4502C9 与磷脂双层的可逆结合，为生物传感器技术提供了潜在的应用。
