通过折叠体扫描方法揭示的抑制剂与组蛋白伴侣ASF1的意外结合模式。
Unexpected binding modes of inhibitors to the histone chaperone ASF1 revealed by a foldamer scanning approach.
作者信息
Perrin Marie E, Li Bo, Mbianda Johanne, Bakail May, André Christophe, Moal Gwenaëlle, Legrand Pierre, Ropars Virginie, Douat Céline, Ochsenbein Françoise, Guichard Gilles
机构信息
Joliot Institute, Commissariat à l'énergie Atomique (CEA), Direction de la Recherche Fondamentale (DRF), CEA Saclay, 91191 Gif-sur-Yvette, France.
Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Saclay, 91190 Gif-sur-Yvette, France.
出版信息
Chem Commun (Camb). 2023 Jul 11;59(56):8696-8699. doi: 10.1039/d3cc01891a.
In the search for foldamer inhibitors of the histone chaperone ASF1, we explored the possibility of substituting four α-residues (≈one helix turn) by 3-urea segments and scanned the sequence of a short α-helical peptide known to bind ASF1. By analysing the impact of the different foldamer replacements within the peptide chain, we uncovered new binding modes of the peptide-urea chimeras to ASF1.
在寻找组蛋白伴侣ASF1的折叠体抑制剂的过程中，我们探索了用3-脲片段取代四个α-残基（约一个螺旋圈）的可能性，并扫描了已知与ASF1结合的短α-螺旋肽的序列。通过分析肽链内不同折叠体取代的影响，我们发现了肽-脲嵌合体与ASF1的新结合模式。
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