Unexpected binding modes of inhibitors to the histone chaperone ASF1 revealed by a foldamer scanning approach-Reference-Cited by-同舟云学术

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

Published:2023 Issue:56 Volume:59 Page:8696-8699
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Perrin Marie E.¹²,Li Bo³^ORCID,Mbianda Johanne³,Bakail May¹²,André Christophe³,Moal Gwenaëlle¹²,Legrand Pierre⁴^ORCID,Ropars Virginie¹²,Douat Céline³^ORCID,Ochsenbein Françoise¹²^ORCID,Guichard Gilles³^ORCID

Affiliation:

1. Joliot Institute, Commissariat à l’énergie Atomique (CEA), Direction de la Recherche Fondamentale (DRF), CEA Saclay, 91191 Gif-sur-Yvette, France

2. Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Saclay, 91190 Gif-sur-Yvette, France

3. Univ. Bordeaux, CNRS, Bordeaux INP, CBMN, UMR 5248, Institut Européen de Chimie et Biologie, F-33600 Pessac, France

4. Synchrotron SOLEIL, L'Orme des Merisiers, 91190 Gif-sur-Yvette, France

Abstract

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.

Funder

Agence Nationale de la Recherche

Alliance Nationale pour les Sciences de la Vie et de la Santé

Fondation ARC pour la Recherche sur le Cancer

Ligue Contre le Cancer

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2023/CC/D3CC01891A

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