Lee M S, Gardner B, Kahn M, Nakanishi H
Molecumetics, Bellevue, WA 98005.
FEBS Lett. 1995 Feb 13;359(2-3):113-8. doi: 10.1016/0014-5793(95)00007-v.
A large number of protein-protein interactions involved turn or loop regions. The excised linear peptides from these regions reveal complex conformational averaging. To circumvent this motional averaging and to stabilize the beta-turn conformation, extensive effort has been devoted to the design of constrained peptidomimetics. Here, we report the three-dimensional solution structure of a 12-membered cyclic peptidomimetic. The structures were calculated from NMR studies performed in chloroform and in water at 263 and 278K, respectively. This 12-membered cyclic scaffolding is part of a program to design and to construct conformationally stable beta-turn peptidomimetics. The impact of the surrounding environment on the conformation of this constrained peptidomimetic is discussed. The general structural features of the cyclic mimetic are retained in both environments; however, the formation of a hydrophobic patch in the aqueous solvent is evident.
大量的蛋白质-蛋白质相互作用涉及转角或环区。从这些区域切除的线性肽显示出复杂的构象平均化。为了规避这种运动平均化并稳定β-转角构象，人们投入了大量精力来设计受限拟肽。在此，我们报告了一种12元环拟肽的三维溶液结构。这些结构分别根据在263K和278K下于氯仿和水中进行的核磁共振研究计算得出。这种12元环支架是设计和构建构象稳定的β-转角拟肽计划的一部分。讨论了周围环境对这种受限拟肽构象的影响。在两种环境中，环模拟物的一般结构特征均得以保留；然而，在水性溶剂中明显形成了一个疏水补丁。
