通过量子力学/分子力学（QM/MM）机理建模确定脂肪酸酰胺水解酶（FAAH）中有效抑制剂的结合方向。
Identification of productive inhibitor binding orientation in fatty acid amide hydrolase (FAAH) by QM/MM mechanistic modelling.
作者信息
Lodola Alessio, Mor Marco, Rivara Silvia, Christov Christo, Tarzia Giorgio, Piomelli Daniele, Mulholland Adrian J
机构信息
Dipartimento Farmaceutico, Università degli Studi di Parma, 43100, Parma, Italy.
出版信息
Chem Commun (Camb). 2008 Jan 14(2):214-6. doi: 10.1039/b714136j. Epub 2007 Oct 19.
Modelling of the mechanism of covalent adduct formation by the inhibitor O-arylcarbamate URB524 in FAAH shows that only one of the two possible inhibitor binding orientations is consistent with the experimentally observed irreversible carbamoylation of the nucleophile serine: this is a potentially crucial insight for designing new covalent inhibitors of this promising drug target.
抑制剂O-芳基氨基甲酸酯URB524在脂肪酸酰胺水解酶（FAAH）中形成共价加合物的机制模型表明，两种可能的抑制剂结合方向中只有一种与亲核丝氨酸的实验观察到的不可逆氨甲酰化一致：这对于设计这种有前景的药物靶点的新型共价抑制剂来说是一个潜在的关键见解。
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