Issue 20, 2018

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 α and X-ray crystallography confirms a helical binding pose.

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

Supplementary files

Article information

Article type
Communication
Submitted
04 abr. 2018
Accepted
23 abr. 2018
First published
26 abr. 2018

Org. Biomol. Chem., 2018,16, 3702-3706

Author version available

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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