The three-dimensional solution structure of a constrained peptidomimetic in water and in chloroform. Observation of solvent induced hydrophobic cluster.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Lee MS,Gardner B,Kahn M,Nakanishi H

doi

10.1016/0014-5793(95)00007-v

subject

Has Abstract

pub_date

1995-02-13 00:00:00

pages

113-8

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(95)00007-V

journal_volume

359

pub_type

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