BIOSYNTHETIC ORIGIN AND RECEPTOR CONFORMATION OF METHIONINE ENKEPHALIN
BIOSYNTHETIC ORIGIN AND RECEPTOR CONFORMATION OF METHIONINE ENKEPHALIN
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DOI：
10.1038/260165a0
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发表时间：
1976-01-01
期刊：
影响因子：
64.8
通讯作者：
SNELL, CR
中科院分区：
文献类型：
--
作者：
BRADBURY, AF;SMYTH, DG;SNELL, CR
最近的报道表明，大脑含有一种具有阿片样活性的内源性肽1 - 3，在垂体中也发现了类似的肽4，5，1 - 3。其中一种脑肽被称为甲硫氨酸脑啡肽，被鉴定为五肽Tyr-Gly-Gly-Phe-Met 6，并且有证据表明，一种次要组分可能含有亮氨酸代替甲硫氨酸。主要序列与促脂素C片段的NH 2-末端相同，促脂素C片段是在猪垂体中大量发现的肽7，8。这表明甲硫氨酸脑啡肽是通过C片段的蛋白水解裂解而在体内产生的。由于脑啡肽被认为直接与阿片类药物竞争脑阿片受体，同时与阿片类药物没有一级结构相似性，因此我们已经寻找并发现了该肽二级结构竞争的基础。
RECENT reports have shown that the brain contains an endogenous peptide with opiate-like activity1–3and similar peptides have been found in the pituitary4,5,13. One of the brain peptides, known as methionine enkephalin, was identified as a pentapeptide Tyr–Gly–Gly–Phe–Met6, and evidence was presented that a minor component may have leucine in place of methionine. The principal sequence is identical to that at the NH2-terminus of lipotropin C fragment, a peptide discovered in substantial quantity in porcine pituitary7,8. This suggests that methionine enkephalin is derivedin vioby proteolytic cleavage of C fragment. Since enkephalin is thought to compete directly with opiates for the brain opiate receptor, while having no primary structure similarity to opiates, we have searched for and found a basis for the competition in a proposed secondary structure for the peptide.