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

Marie E. Perrin; Bo Li; Johanne Mbianda; May Bakail; Christophe André; Gwenaëlle Moal; Pierre Legrand; Virginie Ropars; Céline Douat; Françoise Ochsenbein; Gilles Guichard

doi:10.1039/D3CC01891A

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

Marie E. Perrin,‡^ab Bo Li,

‡^c Johanne Mbianda,‡^c May Bakail,^ab Christophe André,^c Gwenaëlle Moal,^ab Pierre Legrand,

^d Virginie Ropars,^ab Céline Douat,

§^c Françoise Ochsenbein

*^ab and Gilles Guichard

*^c

Author affiliations

* Corresponding authors

^a Joliot Institute, Commissariat à l’énergie Atomique (CEA), Direction de la Recherche Fondamentale (DRF), CEA Saclay, 91191 Gif-sur-Yvette, France
E-mail: francoise.ochsenbein@cea.fr

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

^c Univ. Bordeaux, CNRS, Bordeaux INP, CBMN, UMR 5248, Institut Européen de Chimie et Biologie, F-33600 Pessac, France
E-mail: g.guichard@iecb.u-bordeaux.fr

^d Synchrotron SOLEIL, L'Orme des Merisiers, 91190 Gif-sur-Yvette, France

Abstract

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.

Chemical Communications

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

Abstract

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

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