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Updated: Sep 19, 2025

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第一个选择性IIb类希斯脱乙酶降解剂的开发和表征

Shiyang Zhai1, Irina Honin1, Linda Schäker-Hübner1

  • 1Department of Pharmaceutical and Cell Biological Chemistry, Pharmaceutical Institute, University of Bonn, 53121 Bonn, Germany.

Journal of medicinal chemistry
|June 18, 2025
PubMed
概括

研究人员开发了新的蛋白质溶解向嵌合体 (PROTACs) 来选择性地降解基因组脱乙酶 (HDACs) 6和10. 化合物AP1有效地针对这些IIb类HDAC,而不影响其他HDAC类,为癌症研究提供了一个有前途的工具.

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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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