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

doi:10.1039/c8ob00790j

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 journal › Article › peer-review

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.

Original language	English (US)
Pages (from-to)	3702-3706
Number of pages	5
Journal	Organic and Biomolecular Chemistry
Volume	16
Issue number	20
DOIs	https://doi.org/10.1039/c8ob00790j
State	Published - 2018

ASJC Scopus subject areas

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

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10.1039/c8ob00790j

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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.",

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AU - Speltz, Thomas E.

AU - Mayne, Christopher G.

AU - Fanning, Sean W.

AU - Siddiqui, Zamia

AU - Tajkhorshid, Emad

AU - Greene, Geoffrey L.

AU - Moore, Terry W.

PY - 2018

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AB - 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.

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ER -

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

Abstract

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