Balodis Iu Iu, Vesterman B G, Vosekalna I A, Bobrova I V, Nikiforovich G V
Bioorg Khim. 1985 Nov;11(11):1468-75.
The spatial structure of an enkephaline cycloanalogue Lys-Tyr-Gly-Gly-Phe-Leu--has been investigated by means of energy calculations, fluorescence and CD-spectroscopy. Despite the high conformational mobility of the cycloanalogue, little resemblance exists between its and parent peptide's low-energy structures. Conformational factors for possible mechanisms of interaction between specific enkephalin receptors and cycloanalogue are discussed.
通过能量计算、荧光和圆二色光谱法研究了脑啡肽环类似物Lys-Tyr-Gly-Gly-Phe-Leu-的空间结构。尽管该环类似物具有很高的构象流动性,但其与母体肽的低能量结构之间几乎没有相似之处。讨论了特定脑啡肽受体与环类似物之间相互作用的可能机制的构象因素。