Application of oxime-diversification to optimize ligand interactions within a cryptic pocket of the polo-like kinase 1 polo-box domain

被引：18
作者：
Zhao, Xue Zhi [1 ]
Hymel, David [1 ]
Burke, Terrence R., Jr. [1 ]
机构：
[1] NCI, Biol Chem Lab, Ctr Canc Res, NIH, Frederick, MD 21702 USA
来源：
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2016年 / 26卷 / 20期
基金：
美国国家卫生研究院;
关键词：
Plk1 polo-box domain; Ligand optimization; Oxime ligation; Cryptic binding pocket; PLK1; PEPTIDES; POSITION; ALKYLATION; INHIBITORS; AFFINITY; THERAPY; SURFACE;
D O I：
10.1016/j.bmcl.2016.08.098
中图分类号：
R914 [药物化学];
学科分类号：
100701 ;
摘要：
By a process involving initial screening of a set of 87 aldehydes using an oxime ligation-based strategy, we were able to achieve a several-fold affinity enhancement over one of the most potent previously known polo-like kinase 1 (Plk1) polo-box domain (PBD) binding inhibitors. This improved binding may result by accessing a newly identified auxiliary region proximal to a key hydrophobic cryptic pocket on the surface of the protein. Our findings could have general applicability to the design of PBD-binding antagonists. Published by Elsevier Ltd.
引用
收藏
页码：5009 / 5012
页数：4
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