Centre for Computational Chemistry, School of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK.
J Am Chem Soc. 2013 May 29;135(21):8001-15. doi: 10.1021/ja402016p. Epub 2013 May 16.
Cytochrome P450 enzymes (P450s) are important in drug metabolism and have been linked to adverse drug reactions. P450s display broad substrate reactivity, and prediction of metabolites is complex. QM/MM studies of P450 reactivity have provided insight into important details of the reaction mechanisms and have the potential to make predictions of metabolite formation. Here we present a comprehensive study of the oxidation of three widely used pharmaceutical compounds (S-ibuprofen, diclofenac, and S-warfarin) by one of the major drug-metabolizing P450 isoforms, CYP2C9. The reaction barriers to substrate oxidation by the iron-oxo species (Compound I) have been calculated at the B3LYP-D/CHARMM27 level for different possible metabolism sites for each drug, on multiple pathways. In the cases of ibuprofen and warfarin, the process with the lowest activation energy is consistent with the experimentally preferred metabolite. For diclofenac, the pathway leading to the experimentally observed metabolite is not the one with the lowest activation energy. This apparent inconsistency with experiment might be explained by the two very different binding modes involved in oxidation at the two competing positions. The carboxylate of diclofenac interacts strongly with the CYP2C9 Arg108 side chain in the transition state for formation of the observed metabolite-but not in that for the competing pathway. We compare reaction barriers calculated both in the presence and in the absence of the protein and observe a marked improvement in selectivity prediction ability upon inclusion of the protein for all of the substrates studied. The barriers calculated with the protein are generally higher than those calculated in the gas phase. This suggests that active-site residues surrounding the substrate play an important role in controlling selectivity in CYP2C9. The results show that inclusion of sampling (particularly) and dispersion effects is important in making accurate predictions of drug metabolism selectivity of P450s using QM/MM methods.
细胞色素 P450 酶(P450s)在药物代谢中很重要,并且与药物不良反应有关。P450s 显示出广泛的底物反应性,代谢产物的预测很复杂。P450 反应性的量子力学/分子力学研究提供了对反应机制重要细节的深入了解,并有可能对代谢产物的形成进行预测。在这里,我们对一种主要的药物代谢 P450 同工酶 CYP2C9 氧化三种广泛使用的药物化合物(S-布洛芬、双氯芬酸和 S-华法林)进行了全面研究。在不同的药物中,在多个途径上,对每种药物的不同可能代谢部位的铁-氧物种(化合物 I)的底物氧化反应势垒,在 B3LYP-D/CHARMM27 水平上进行了计算。在布洛芬和华法林的情况下,具有最低活化能的过程与实验中首选的代谢物一致。对于双氯芬酸,导致实验观察到的代谢物的途径不是具有最低活化能的途径。这种与实验的明显不一致可能是由于在两个竞争位置氧化中涉及的两种非常不同的结合模式造成的。双氯芬酸的羧酸与 CYP2C9 Arg108 侧链在形成观察到的代谢物的过渡态中强烈相互作用,但在竞争途径的过渡态中没有相互作用。我们比较了在存在和不存在蛋白质的情况下计算的反应势垒,并观察到在所有研究的底物中,包含蛋白质可以显著提高选择性预测能力。与在气相中计算的相比,包含蛋白质计算的势垒通常更高。这表明,围绕底物的活性部位残基在控制 CYP2C9 中的选择性方面起着重要作用。结果表明,在使用 QM/MM 方法准确预测 P450 药物代谢选择性时,包括采样(特别是)和弥散效应非常重要。