Unexpected binding modes of inhibitors to the histone chaperone ASF1 revealed by a foldamer scanning approach - Archive ouverte HAL
Article Dans Une Revue Chemical Communications Année : 2023

Unexpected binding modes of inhibitors to the histone chaperone ASF1 revealed by a foldamer scanning approach

Marie Perrin
  • Fonction : Auteur
Pierre Legrand

Résumé

We used foldamer inserts to scan the sequence of a peptide ligand of the histone chaperone ASF1, and interrogate its interaction with the protein surface. Our results revealed the structural plasticity of the chimeras and new binding modes to ASF1.

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Chimie
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Dates et versions

hal-04700842 , version 1 (18-09-2024)

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Citer

Marie Perrin, Bo Li, Johanne Mbianda, May Bakail, Christophe André, et al.. Unexpected binding modes of inhibitors to the histone chaperone ASF1 revealed by a foldamer scanning approach. Chemical Communications, 2023, 59 (56), pp.8696-8699. ⟨10.1039/D3CC01891A⟩. ⟨hal-04700842⟩
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