A "cross-stitched" peptide with improved helicity and proteolytic stability

Org Biomol Chem. 2018 May 23;16(20):3702-3706. doi: 10.1039/c8ob00790j.

Abstract

A new computational approach to obtain quantitative energy profiles for helix folding was used in the design of orthogonal hydrocarbon and lactam bicyclic peptides. The proteolytically stable, "cross-stitched" peptide SRC2-BCP1 shows nanomolar affinity for estrogen receptor α and X-ray crystallography confirms a helical binding pose.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Binding Sites
  • Estrogen Receptor alpha / metabolism
  • Models, Molecular
  • Peptides / chemistry*
  • Peptides / metabolism*
  • Protein Conformation, alpha-Helical
  • Proteolysis*

Substances

  • Estrogen Receptor alpha
  • Peptides