A "cross-stitched" peptide with improved helicity and proteolytic stabilityElectronic supplementary information (ESI) available. See DOI: 10.1039/c8ob00790j

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 cry...

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Main Authors: Speltz, Thomas E, Mayne, Christopher G, Fanning, Sean W, Siddiqui, Zamia, Tajkhorshid, Emad, Greene, Geoffrey L, Moore, Terry W
Format: Article
Language:English
Online Access:Get full text
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Summary: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. Peptide "cross-stitching" maintains binding affinity and can enhance helical and proteolytic stability.
ISSN:1477-0520
1477-0539
DOI:10.1039/c8ob00790j