| Literature DB >> 14971886 |
Yasuki Yamada1, Kenji Mizutani, Yasuhiro Mizusawa, Yoshiji Hantani, Makoto Tanaka, Yuko Tanaka, Masaki Tomimoto, Makoto Sugawara, Norio Imai, Hideki Yamada, Nobuyuki Okajima, Jun-ichi Haruta.
Abstract
The discovery of small and potent peptide antagonists of the corticotropin-releasing factor (CRF) receptor is described. Through the structure-activity relationship studies of 12-amino acid peptide corresponding to the C-terminal residues of astressin, we assumed that a particular surface of the alpha-helix was important for binding to the receptor. The small peptide containing d-Ala31 and cyclohexylalanine38 on that surface was as potent as astressin in binding to the CRF receptor and showed significant ACTH suppression when administered to rats.Entities:
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Year: 2004 PMID： 14971886 DOI： 10.1021/jm034180+
Source DB: PubMed Journal: J Med Chem ISSN： 0022-2623 Impact factor: 7.446