权益分类	功能权益	普通用户	{{item.name}}会员
{{category.name}}	{{benefitItem.name}}

Ultraviolet Resonance Raman Spectroscopic Study on the Conformation of Enkephalin and Binding Mode to Receptors

脑啡肽构象及受体结合方式的紫外共振拉曼光谱研究

基本信息

批准号：
01470142
负责人：
TAKEUCHI Hideo
金额：
$ 0.77万
依托单位：
Tohoku University
依托单位国家：
日本
项目类别：
Grant-in-Aid for General Scientific Research (B)
财政年份：
1989
资助国家：
日本
起止时间：
1989 至 1990
项目状态：
已结题

来源：
https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-01470142/
关键词：
Enkephalin Opioid Receptor UV resonance Raman spectroscopy ラマン分光赤外分光 βタ-ン

项目摘要

We have studied the ultraviolet (213- and 240-nm) resonance Raman (UVRR) spectra of Met-enkephalin, Leu-enkephalin, and [Trp^4] Met-enkephalin incorporated into dilauroylphatidylcholine liposomes. The analysis of the spectra based on the data of model compounds obtained previously has provided several pieces of important information on the binding mode of enkephalin to the lipid bilayers. A delta-type opioid receptor has been extracted from rat brain and purified. The structure of the receptor has been investigated by UVRR and circular dichroism spectroscopy. The results obtained are as follows :1. Every enkephalin mentioned above exists as an ensemble of various extended conformers in aqueous solution, whereas it takes a folded conformation in the lipid-bound state.2. The Tyr side chain is inserted into the membrane hydrophobic interior, but the Phe side chain is located in the polar surface region or exposed to the aqueous phase.3. The degree of insertion of Tyr into the membrane is smaller for Leu-enkephalin than the other two.4. The deeper the Tyr is buried, the higher the affinity and activity of the peptide.5. The membrane environment is considered to play a role in protecting the N-terminal Tyr form degradation in tissues.6. The mainchain of the delta-opioid receptor is largely in the beta-sheet structure and the protein does not contain many aromatic residues, particularly Tyr and Typ.

我们研究了甲硫氨酸脑啡肽、亮氨酸脑啡肽和[Trp^4]甲硫氨酸脑啡肽与双月桂酰磷脂酰胆碱脂质体的紫外(213 nm和240 nm)共振拉曼光谱。根据先前获得的模型化合物的数据进行的光谱分析，为脑啡肽与脂质双层的结合方式提供了几条重要的信息。从大鼠脑中提取并纯化了一种Delta型阿片受体。用UVRR和圆二色谱研究了该受体的结构。所得结果如下：1.上述脑啡肽在水溶液中均以各种延伸构象的集合形式存在，而在脂结合状态下则以折叠构象形式存在。Tyr侧链插入膜疏水内部，而Phe侧链位于膜的极性表面区或暴露在水相中。亮氨酸脑啡肽的酪氨酸插入膜的程度比其他两种小。酪氨酸埋得越深，多肽的亲和力和活性越高。膜环境被认为在保护N-末端Tyr在组织中不被降解中起作用。阿片受体的主链主要在β-折叠结构中，蛋白质不含许多芳香族残基，特别是Tyr和Typ。