E-resources
Peer reviewed
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Perrin, Marie E; Li, Bo; Mbianda, Johanne; Bakail, May; André, Christophe; Moal, Gwenaëlle; Legrand, Pierre; Ropars, Virginie; Douat, Céline; Ochsenbein, Françoise; Guichard, Gilles
Chemical communications (Cambridge, England), 07/2023, Volume: 59, Issue: 56Journal Article
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. 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.
