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

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 - Jan 1 2018

ASJC Scopus subject areas

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

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10.1039/c8ob00790j

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Speltz, T. E., Mayne, C. G., Fanning, S. W., Siddiqui, Z., Tajkhorshid, E., Greene, G. L., & Moore, T. W. (2018). A "cross-stitched" peptide with improved helicity and proteolytic stability. Organic and Biomolecular Chemistry, 16(20), 3702-3706. https://doi.org/10.1039/c8ob00790j

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AU - Greene, Geoffrey L.

AU - Moore, Terry W.

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