肉豆蔻酰转移酶喹啉抑制剂的结构导向优化
Structure-guided optimization of quinoline inhibitors of -myristoyltransferase.
作者信息
Goncalves Victor, Brannigan James A, Laporte Alice, Bell Andrew S, Roberts Shirley M, Wilkinson Anthony J, Leatherbarrow Robin J, Tate Edward W
机构信息
Department of Chemistry , Imperial College London , London SW7 2AZ , UK . Email:
Structural Biology Laboratory , Department of Chemistry , University of York , York YO10 5DD , UK.
出版信息
Medchemcomm. 2017 Jan 1;8(1):191-197. doi: 10.1039/c6md00531d. Epub 2016 Nov 11.
The parasite is the most widely distributed cause of recurring malaria. -Myristoyltransferase (NMT), an enzyme that catalyses the covalent attachment of myristate to the N-terminal glycine of substrate proteins, has been described as a potential target for the treatment of this disease. Herein, we report the synthesis and the structure-guided optimization of a series of quinolines with balanced activity against both and -myristoyltransferase (NMT).
该寄生虫是复发性疟疾分布最广泛的病因。N-肉豆蔻酰转移酶（NMT）是一种催化肉豆蔻酸共价连接到底物蛋白N端甘氨酸的酶，已被描述为治疗这种疾病的潜在靶点。在此，我们报告了一系列对α-和β-N-肉豆蔻酰转移酶（NMT）具有平衡活性的喹啉的合成及基于结构的优化。
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