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A "cross-stitched" peptide with improved helicity 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 ? and X-ray crystallography confirms a helical binding pose.

SUBMITTER: Speltz TE

PROVIDER: S-EPMC5993042 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature

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

Speltz Thomas E TE Mayne Christopher G CG Fanning Sean W SW Siddiqui Zamia Z Tajkhorshid Emad E Greene Geoffrey L GL Moore Terry W TW

Organic & biomolecular chemistry 20180501 20

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. ...[more]

PMID: 29725689

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