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

In the search for foldamer inhibitors of the histone chaperone ASF1, we explored the possibility of substituting four & alpha;-residues (& AP;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.

Automated summary

In this study, we investigated the substitution of 4 α-residues with 3-urea segments in a short α-helical peptide known to bind ASF1. By analyzing the effects of different foldamer replacements, we discovered new binding modes for the peptide-urea chimeras with ASF1.