@article{oai:tohoku-mpu.repo.nii.ac.jp:00000194,
 author = {河野, 奨 and Kawano, Susumu and 伊藤, 里沙 and Ito, Risa and 西山, 美春 and Nishiyama, Miharu and 久保, 麻衣 and Kubo, Mai and 松島, 知子 and Matsushima, Tomoko and 安保, 明博 and Ambo, Akihiro and 佐々木, 有亮 and Sasaki, Yusuke},
 issue = {53},
 journal = {東北薬科大学研究誌, Journal of Tohoku Pharmaceutical University},
 month = {Dec},
 note = {Receptor binding properties and antinociceptive activities of chimeric peptides linked by spacers were investigated. The peptides consisted of the μ-opioid receptor ligand dermorphin (Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH_2) or its analog YRFB (Tyr-D-Arg-Phe-βAla-NH_2) linked to the ORL-1 receptor ligand Ac-Arg-Tyr-Tyr-Arg-Ile-Lys-NH_2 (Ac-RYYRIK-NH_2). All chimeric peptides were found to possess high receptor binding affinities for both μ-opioid and ORL-1 receptors in mouse brain membranes. In particular, chimeric peptide 2, which consists of dermorphin and Ac-RYYRIK-NH_2 connected by a long spacer, had high binding affinities toward both receptors. In the tail-flick test following intracerebroventricular (i.c.v.) administration of chimeric peptides containing the YRFB sequence (3 and 4) unexpectedly showed much less potent antinociceptive activity (ED_<5O>>100 pmole/mouse). These results suggest the involvement of nociceptin-like effects of the Ac-RYYRIK pharmacophore in the peptides, and the regulation of μ-opioid receptor-mediated antinociception in brain. The present chimeric peptides (2, 3 and 4) may be useful as pharmacological tools for studies on μ-opioid receptor/ORL-1 receptor heterodimers.},
 pages = {85--91},
 title = {μ-オピオイド受容体アゴニストとORL-1受容体アンタゴニストから成るキメラペプチドの受容体親和性と鎮痛活性},
 year = {2006},
 yomi = {カワノ, ススム and イトウ, リサ and ニシヤマ, ミハル and クボ, マイ and マツシマ, トモコ and アンボ, アキヒロ and ササキ, ユウスケ}
}