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Issue 20, 2018
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A “cross-stitched” peptide with improved helicity and proteolytic stability

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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.

Graphical abstract: A “cross-stitched” peptide with improved helicity and proteolytic stability

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Publication details

The article was received on 04 Apr 2018, accepted on 23 Apr 2018 and first published on 26 Apr 2018


Article type: Communication
DOI: 10.1039/C8OB00790J
Citation: Org. Biomol. Chem., 2018,16, 3702-3706
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    A “cross-stitched” peptide with improved helicity and proteolytic stability

    T. E. Speltz, C. G. Mayne, S. W. Fanning, Z. Siddiqui, E. Tajkhorshid, G. L. Greene and T. W. Moore, Org. Biomol. Chem., 2018, 16, 3702
    DOI: 10.1039/C8OB00790J

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