2002年
Design and Synthesis of novel tetra-peptide motilin agonists
Bioorganic and Medicinal Chemistry
- ,
- ,
- ,
- ,
- ,
- ,
- ,
- 巻
- 10
- 号
- 6
- 開始ページ
- 1805
- 終了ページ
- 1811
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/S0968-0896(02)00027-5
A series of novel tetra-peptide motilin agonists, having the general structure H-Phe-Val-X-Ile-NH2, were designed, on the basis of structure-activity relationship studies of motilin. Peptides, in which X is a side chain substituted tryptophan residue, have agonistic activity. H-Phe-Val-Trp(2′-CH2CH2OH)-Ile-NH2(7), H-Phe-Val-Trp(2′-SCH3)-Ile-NH2(8), and H-Phe-Val-Trp(2′-SCH2CH2CH3)-Ile-NH 2 (9), showed an EC50 for contractile activity in the rabbit smooth muscle of 14.1±3.2, 12.9±4.1, and 4.6±1.6 μM, respectively. Interaction of the tryptophan aliphatic side chain with motilin receptor appears to influence the signal transduction via motilin receptor. © 2002 Elsevier Science Ltd. All rights reserved.
- リンク情報
- ID情報
-
- DOI : 10.1016/S0968-0896(02)00027-5
- ISSN : 0968-0896
- PubMed ID : 11937338
- SCOPUS ID : 0036009877