SPECIFIC RECEPTOR FOR THE OPIOID PEPTIDE DYNORPHIN - STRUCTURE-ACTIVITY-RELATIONSHIPS
SPECIFIC RECEPTOR FOR THE OPIOID PEPTIDE DYNORPHIN - STRUCTURE-ACTIVITY-RELATIONSHIPS
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DOI：
10.1073/pnas.78.10.6543
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发表时间：
1981-01-01
期刊：
影响因子：
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通讯作者：
GOLDSTEIN, A
中科院分区：
文献类型：
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作者：
CHAVKIN, C;GOLDSTEIN, A
研究了豚鼠回肠肌间神经丛中阿片肽强啡肽的高效价和阿片受体特异性的结构特征。从强啡肽-(1-13)中连续去除COOH末端的氨基酸表明，赖氨酸-13、赖氨酸-11和精氨酸-7对效力有重要贡献。去掉NH2末端的酪氨酸，生物活性就消失了。其他几个结构修饰影响了效力：D-丙氨酸取代甘氨酸-2降低了强啡肽-(1-13)酰胺、-(1-11)和-(1-10)的效力；COOH末端的甲酯化提高了强啡肽-(1-12)、-(1-10)、-(1-9)、-(1-8)和-(1-7)的效力。在强啡肽序列中，赖氨酸-11和精氨酸-7对于与强啡肽受体相互作用的选择性是重要的，这与.MU是不同的。该组织中的受体。
The structural features responsible for the high potency and opiate receptor specificity of the opioid peptide dynorphin in the guinea pig ileum myenteric plexus were examined. Successive removal of COOH-terminal amino acids from dynorphin-(1-13) demonstrated important contributions of lysine-13, lysine-11, and arginine-7 to the potency. Removal of the NH2-terminal tyrosine abolished the biologic activity. Several other structural modifications affected potency: substitution of D-alanine for glycine-2 reduced the potencies of dynorphin-(1-13) amide, -(1-11), and -(1-10); and methyl esterification of the COOH terminus enhanced the potencies of dynorphin-(1-12), -(1-10), -(1-9), -(1-8) and -(1-7). Within the dynorphin sequence, lysine-11 and arginine-7 were important for selectivity of interaction with the dynorphin receptor, which is distinguishable from the .mu. receptor in this tissue.