Covalent and Noncovalent Targeting of the Tcf4/β-Catenin Strand Interface with β-Hairpin Mimics

ACS Chem Biol. 2021 Aug 20;16(8):1518-1525. doi: 10.1021/acschembio.1c00389. Epub 2021 Jul 21.

Abstract

β-Strands are a fundamental component of protein structure, and these extended peptide regions serve as binding epitopes for numerous protein-protein complexes. However, synthetic mimics that capture the conformation of these epitopes and inhibit selected protein-protein interactions are rare. Here we describe covalent and noncovalent β-hairpin mimics of an extended strand region mediating the Tcf4/β-catenin interaction. Our efforts afford a rationally designed lead for an underexplored region of β-catenin, which has been the subject of numerous ligand discovery campaigns.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Escherichia coli / chemistry
  • Escherichia coli Proteins / metabolism
  • Peptides, Cyclic / chemistry
  • Peptides, Cyclic / metabolism*
  • Protein Binding / drug effects*
  • Protein Conformation
  • Transcription Factor 4 / metabolism*
  • beta Catenin / metabolism*

Substances

  • Escherichia coli Proteins
  • Peptides, Cyclic
  • Transcription Factor 4
  • beta Catenin