8cj2: Difference between revisions
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In the search for foldamer inhibitors of the histone chaperone ASF1, we explored the possibility of substituting four alpha-residues ( approximately one helix turn) by 3-urea segments and scanned the sequence of a short alpha-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. | In the search for foldamer inhibitors of the histone chaperone ASF1, we explored the possibility of substituting four alpha-residues ( approximately one helix turn) by 3-urea segments and scanned the sequence of a short alpha-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. | ||
Unexpected binding modes of inhibitors to the histone chaperone ASF1 revealed by a foldamer scanning approach.,Perrin ME, Li B, Mbianda J, Bakail M, Andre C, Moal G, Legrand P, Ropars V, Douat C, Ochsenbein F, Guichard G Chem Commun (Camb). 2023 | Unexpected binding modes of inhibitors to the histone chaperone ASF1 revealed by a foldamer scanning approach.,Perrin ME, Li B, Mbianda J, Bakail M, Andre C, Moal G, Legrand P, Ropars V, Douat C, Ochsenbein F, Guichard G Chem Commun (Camb). 2023 Jul 11;59(56):8696-8699. doi: 10.1039/d3cc01891a. PMID:37347155<ref>PMID:37347155</ref> | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
