Premium
The three‐dimensional solution structure of a constrained peptidomimetic in water and in chloroform observation of solvent induced hydrophobic cluster
Author(s) -
Lee Min S.,
Gardner Benjamin,
Kahn Michael,
Nakanishi Hiroshi
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00007-v
Subject(s) - peptidomimetic , chloroform , chemistry , aqueous solution , solvent , stereochemistry , computational chemistry , organic chemistry , peptide , biochemistry
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.