Influence of Macrocyclization on Allosteric, Juxtamembrane-Derived, Stapled Peptide Inhibitors of the Epidermal Growth Factor Receptor (EGFR) | Zendy

Julie K.-L. Sinclair | Zendy; Alanna Schepartz | Zendy

Open Access

Influence of Macrocyclization on Allosteric, Juxtamembrane-Derived, Stapled Peptide Inhibitors of the Epidermal Growth Factor Receptor (EGFR)

Author(s) -

Julie K.-L. Sinclair,

Alanna Schepartz

Publication year - 2014

Publication title -

organic letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.94

H-Index - 239

eISSN - 1523-7060

pISSN - 1523-7052

DOI - 10.1021/ol502426b

Subject(s) - chemistry , allosteric regulation , epidermal growth factor receptor , epidermal growth factor , peptide , receptor , erbb3 , allosteric modulator , combinatorial chemistry , stereochemistry , cancer research , microbiology and biotechnology , biochemistry , biology

The hydrocarbon-stapled peptide E1(S) allosterically inhibits the kinase activity of the epidermal growth factor receptor (EGFR) by blocking a distant but essential protein-protein interaction: a coiled coil formed from the juxtamembrane segment (JM) of each member of the dimeric partnership.1 Macrocyclization is not required for activity: the analogous unstapled (but alkene-bearing) peptide is equipotent in cell viability, immunoblot, and bipartite display experiments to detect coiled coil formation on the cell surface.

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