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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]

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