Journal
BIOORGANIC & MEDICINAL CHEMISTRY
Volume 20, Issue 19, Pages 5730-5737Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2012.08.013
Keywords
EGF receptor; Dimerization; Inhibitor; Cyclic peptide; Retro-Inverso modification; A431 cell
Funding
- 21st Century COE Program
- Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan
- Japan Society for the Promotion of Science (JSPS)
- Naito Foundation
- Grants-in-Aid for Scientific Research [24590134] Funding Source: KAKEN
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Structure-activity relationships of cyclic peptides mimicking the beta-hairpin structure of the 'dimerization arm' at residues 242-259 of the EGF receptor are examined. Cyclic peptides containing the arm head of the beta-hairpin loop showed inhibitory activity toward the EGF receptor's dimerization. Cyclic peptides containing a Retro-Inverso sequence of the dimerization arm showed clear inhibitory effects on the dimerization in vitro and efficiently suppressed the proliferation of A431 cells, which abundantly express the EGF receptor on their surface. The effects at a specific hydrophobic site of the loop structure were expected to enhance the interactions with the receptor. (C) 2012 Elsevier Ltd. All rights reserved.
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