Work

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

Year: 2018

Type: 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.

Source: Organic & Biomolecular Chemistry

DOI: 10.1039/c8ob00790j

Authors: Thomas E. Speltz, Christopher G. Mayne, Sean W. Fanning, Zamia Siddiqui, Emad Tajkhorshid, Geoffrey L. Greene, Terry W. Moore

Institutions: University of Illinois Chicago, University of Illinois Urbana-Champaign, University of Chicago

Language: English

Topic: Chemical Synthesis and Analysis

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Science Foundation, National Institutes of Health, National Institute of General Medical Sciences, National Center for Complementary and Integrative Health

Awards: G1104241873, G162808528, G3226045097, G3780455790, G7712827029, G9000013398, G9000016563

OpenAlex ID: W2802585333

FWCI: 1.677

Cites: 29

Cited by: 39

Related to: 10