Perlikowska Renata, Fichna Jakub, Janecka Anna
Zakład Chemii Biomolekularnej, Uniwersytet Medyczny w Łodzi, Łódź, Poland.
Postepy Biochem. 2009;55(4):388-94.
Two endogenous opioid peptides with extremely high mu-opioid receptor affinity and selectivity, endomorphin-1 and endomorphin-2, were: discovered and isolated from the mammalian brain in 1997. Endomorphins are amidated tetrapeptides, structurally different from so called typical opioids: enkephalins, dynorphins and endorphins. A protein precursor of endomorphins and a gene encoding their sequence remain unknown. Endomorphins are unable to cross the blood-brain barrier because of their low hydrophobicity. In animal models, these peptides turned out to be very potent in relieving neuropathic and inflammatory pain. In comparison with morphine, a prototype opioid receptor ligand, endomorphins produces less undesired side effects. In this article we describe the discovery of endomorphins, their cellular localization and functions in the organism, as well as their structure-activity relationships and biodegradation pathways.
1997年，两种对μ-阿片受体具有极高亲和力和选择性的内源性阿片肽——内吗啡肽-1和内吗啡肽-2，从哺乳动物大脑中被发现并分离出来。内吗啡肽是酰胺化的四肽，在结构上不同于所谓的典型阿片类物质：脑啡肽、强啡肽和内啡肽。内吗啡肽的蛋白质前体及其编码序列的基因仍然未知。由于内吗啡肽的疏水性较低，它们无法穿过血脑屏障。在动物模型中，这些肽在缓解神经性和炎性疼痛方面表现出很强的效力。与阿片受体配体原型吗啡相比，内吗啡肽产生的不良副作用更少。在本文中，我们描述了内吗啡肽的发现、它们在机体中的细胞定位和功能，以及它们的构效关系和生物降解途径。
