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Recognition of ASF1 by Using Hydrocarbon-Constrained Peptides

  • May Bakail
  • , Silvia Rodriguez-Marin
  • , Zsófia Hegedüs
  • , Marie E. Perrin
  • , Françoise Ochsenbein
  • , Andrew J. Wilson
  • Université Paris-Saclay
  • INSERM U869
  • School of Chemistry
  • University of Leeds
  • Astbury Centre for Structural Molecular Biology

Research output: Contribution to journal › Article › peer-review

8 Citations (Scopus)

Abstract

Inhibiting the histone H3–ASF1 (anti-silencing function 1) protein–protein interaction (PPI) represents a potential approach for treating numerous cancers. As an α-helix-mediated PPI, constraining the key histone H3 helix (residues 118–135) is a strategy through which chemical probes might be elaborated to test this hypothesis. In this work, variant H3 118–135 peptides bearing pentenylglycine residues at the i and i+4 positions were constrained by olefin metathesis. Biophysical analyses revealed that promotion of a bioactive helical conformation depends on the position at which the constraint is introduced, but that the potency of binding towards ASF1 is unaffected by the constraint and instead that enthalpy–entropy compensation occurs.

Original languageEnglish
Pages (from-to)891-895
Number of pages5
JournalChemBioChem
Volume20
Issue number7
DOIs
Publication statusPublished - 1 Apr 2019
Externally publishedYes

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

  1. SDG 3 - Good Health and Well-being
    SDG 3 Good Health and Well-being

Keywords

  • chemical biology
  • constrained peptides
  • histone chaperones
  • protein surface recognition
  • protein–protein interactions

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