The three‐dimensional solution structure of a constrained peptidomimetic in water and in chloroform observation of solvent induced hydrophobic cluster

FEBS Letters

Lee, Min S.¹  Kahn, Michael¹  Nakanishi, Hiroshi¹  Gardner, Benjamin¹ 

[1] Molecumetics, Bellevue, WA 98005, USA

关键词: Peptidomimetic;    Hydrophobic cluster;    Solution structure;    Nuclear magnetic resonance;    Solvent effect;    NMR;    nuclear magnetic resonance;    DG;    Distance geometry;    SA;    Simulated annealing;    ppm;    parts per million;    SASA;    solvent accessible surface area;   

DOI  :  10.1016/0014-5793(95)00007-V

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A large number of protein-protein interactions involve turn or loop regions. The excised linear peptides from these regions reveal complex conformational averaging. To circumvent this motional averaging and to stabilize the β-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 β-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.

【 授权许可】

Unknown