Structure-based design of conformationally constrained cyclic peptidomimetics to target the MLLI-WDR5 protein-protein interaction as inhibitors of the MLL1 methyltransferase activity

We described herein structure-based design, synthesis and evaluation of conformationally constrained, cyclic peptidomimetics to block the MLL1-WDR5 protein-protein interaction as inhibitors of the MLL1 histone methyltransferase activity. Our study has yielded cyclic peptidomimetics with very high bi...

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Bibliographic Details
Published in:中国化学快报：英文版 2015 (4), p.455-458
Main Author: Hacer Karatas Shirley Y. Lee Elizabeth C. Townsend Fang Cao Jing xu Denzil Bernard Liu Liu Yali Dou Shaomeng Wang
Format: Article
Language:English
Subjects:
基础
抑制剂
构象
环状
结构
蛋白质相互作用
设计
酶活性
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Summary:We described herein structure-based design, synthesis and evaluation of conformationally constrained, cyclic peptidomimetics to block the MLL1-WDR5 protein-protein interaction as inhibitors of the MLL1 histone methyltransferase activity. Our study has yielded cyclic peptidomimetics with very high binding affinities to WDR5 （Ki values 〈1 nmol/L） and function as antagonists of the MLL1 histone methyltransferase activity.
ISSN:1001-8417
1878-5964