Nikiforovich G V, Balodis J
Institute of Organic Synthesis, Latvian SSR Academy of Sciences, Riga.
FEBS Lett. 1988 Jan 25;227(2):127-30. doi: 10.1016/0014-5793(88)80882-2.
Sets of low-energy structures were determined by energy calculations for two cyclic analogues of enkephalin (Ek), [D-Pen2, D-Pen5]-Ek and [D-Pen2, L-Pen5]-Ek, possessing the highest specificity towards delta-opioid receptors. Comparison of mutual spatial orientations of the alpha-amino group and aromatic moieties of the Tyr and Phe residues permitted one to suggest a model for the delta-receptor-bound conformation of enkephalin-related peptides. The model involves a pronounced gamma-like turn of the peptide backbone centred on the Gly3 residue.
通过对脑啡肽（Ek）的两种环类似物[D-青霉胺2，D-青霉胺5]-Ek和[D-青霉胺2，L-青霉胺5]-Ek进行能量计算，确定了低能量结构集，这两种类似物对δ-阿片受体具有最高的特异性。比较酪氨酸（Tyr）和苯丙氨酸（Phe）残基的α-氨基和芳香部分的相互空间取向，有助于提出一种与脑啡肽相关肽的δ-受体结合构象模型。该模型涉及以甘氨酸3（Gly3）残基为中心的肽主链明显的γ-样转折。
