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

Thomas E. Speltz, Christopher G. Mayne, Sean W. Fanning, Zamia Siddiqui, Emad Tajkhorshid, Geoffrey L. Greene, Terry W. Moore

Research output: Contribution to journalArticle


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.

Original languageEnglish (US)
Pages (from-to)3702-3706
Number of pages5
JournalOrganic and Biomolecular Chemistry
Issue number20
StatePublished - Jan 1 2018

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry

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    Speltz, T. E., Mayne, C. G., Fanning, S. W., Siddiqui, Z., Tajkhorshid, E., Greene, G. L., & Moore, T. W. (2018). A "cross-stitched" peptide with improved helicity and proteolytic stability. Organic and Biomolecular Chemistry, 16(20), 3702-3706. https://doi.org/10.1039/c8ob00790j