| 标题 |
 A Review of Stapled Peptides and Small Molecules to Inhibit Protein-Protein Interactions in Cancer 相关领域
拟肽
氨基酸
小分子
肽序列
生物化学
化学
蛋白质-蛋白质相互作用
肽
功能（生物学）
细胞生物学
生物
计算生物学
基因
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| 网址 | |
| DOI |
10.2174/0929867323666160627103134
doi
|
| 其它 |
Author:Vidhya V Iyer PMID: 27356541 Abstract Disruption of binding of two or more molecules to a protein surface is a common basis of inhibition of many biological activities. Smallmolecule inhibitors, antibodies, proteins, and peptidomimetics have been examined as ways to antagonize receptor activity. The peptide α-helix plays a crucial role in the function of many proteins. Hence, much effort has been invested in mimicking α-helices at the binding interface of two proteins to competitively inhibit their interactions. Peptide stapling involves choosing two amino acids on the same face of a native peptide sequence for substitution with non-native amino acids whose side chains can be "stapled" together. The focus of this review is to survey the prevalence in literature of stapled peptides and small-molecule antagonists of interactions of selected mammalian cancer targets, such as β-catenin, BH3-only members of the Bcl-2 family of proteins, eIF4E/G, estrogen receptor complexes, EZH2, Mdm2, Notch, p110α, and survivin. The increasing interest in protein targets currently considered to be "undruggable" with greater selectivity for existing targets, with the goal of overcoming the omnipresent problem of resistance, could be served well by utilizing information about protein-protein interactions to develop both small-molecule and stapled peptide inhibitors. |
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2020-05-24 18:03:22 发布，悬赏 10 积分
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