Inhibitory effect of a dimerization-arm-mimetic peptide on EGF receptor activation.

Abstract

A cyclic decapeptide was chemically synthesized that mimics the loop structure of a beta-hairpin arm of the EGF receptor, which is highly involved in receptor dimerization upon activation by ligand binding. This peptide was revealed to reduce dimer formation of the receptor in a detergent-solubilized extract of epidermoid carcinoma A431 cells and to inhibit receptor autophosphorylation at less than 10 microM in the intact cells.

• Authors: Takaaki Mizuguchi, Hiromasa Uchimura, Taeko Kakizawa, Tooru Kimura, Shigeyuki Yokoyama, Yoshiaki Kiso, Kazuki Saito
• Journal: Bioorganic & medicinal chemistry letters (Bioorg Med Chem Lett) Vol. 19 Issue 12 Pg. 3279-82 (Jun 15 2009) ISSN: 1464-3405 [Electronic] England
• PMID: 19419869 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Peptides, Cyclic
• ErbB Receptors

Topics

• Cell Line, Tumor
• Drug Design
• ErbB Receptors (antagonists & inhibitors, chemistry)
• Humans
• Molecular Mimicry
• Peptides, Cyclic (chemical synthesis, chemistry, pharmacology)
• Protein Multimerization (drug effects)
• Structure-Activity Relationship