著者

土井 光暢 石田 寿昌

出版者

一般社団法人 日本生物物理学会

雑誌

生物物理 (ISSN:05824052)

巻号頁・発行日

vol.30, no.3, pp.120-126, 1990-05-25 (Released:2010-01-07)

参考文献数

20

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Enkephalin is a morphine-like pentapeptide: Tyr-Gly-Gly-Phe-Xxx, Xxx=Met or Leu. To consider the relationship between the enkephalin conformation and the opioid receptor, the crystal structures of enkephalin analogues were analyzed by the X-ray diffraction method, and two characteristic forms were observed as the fundamental conformation of enkephalin, One is the β-turn structllre and the other the antiparallelly extended dimer (ED) structure. From the NMR and CD spectral studies, it was suggested that the β-turn and ED structures of enkephalin are the most probable conformations for the binding to μ-and δ-receptors, respectively. Further, the molecular-dynamics simulations indicated that these conformation are both advantageous in energetical term. Based on the insight of the enkephalin conformation, it was attempted to convert the μ-selective morphine toward δ-affinitive ligand by the dimerization.