A "cross-stitched" peptide with improved helicity and proteolytic stability. Issue 20 (4th May 2018)

• Record Type: Journal Article
• Authors: Speltz, Thomas E.; Mayne, Christopher G.; Fanning, Sean W.; Siddiqui, Zamia; Tajkhorshid, Emad; Greene, Geoffrey L.; Moore, Terry W.
• Is Part Of: Organic & biomolecular chemistry. Volume 16:Issue 20(2018)
• Page Start: 3702
• Page End: 3706
• Publication Date: 2018-05-04
• Subjects: Chemistry, Organic -- Periodicals; Bioorganic chemistry -- Periodicals; Chemistry, Physical organic -- Periodicals; 547
• DOI: 10.1039/c8ob00790j
• Languages: English
• ISSNs: 1477-0520

Abstract

Abstract : Peptide "cross-stitching" maintains binding affinity and can enhance helical and proteolytic stability. 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.