THE 3-DIMENSIONAL SOLUTION STRUCTURE OF A CONSTRAINED PEPTIDOMIMETIC IN WATER AND IN CHLOROFORM - OBSERVATION OF SOLVENT-INDUCED HYDROPHOBIC CLUSTER

A large number of protein-protein interactions involve turn or loop re gions, The excised linear peptides from these regions reveal complex c onformational averaging. To circumvent this motional averaging and to stabilize the beta-turn conformation, extensive effort has been devote d to the design of constrained peptidomimetics. Here, we report the th ree-dimensional solution structure of a 12-membered cyclic peptidomime tic. The structures were calculated from NMR studies performed in chlo roform and in water at 263 and 278K, respectively, This 12-membered cy clic scaffolding is part of a program to design acid to construct conf ormationally stable beta-turn peptidomimetics. The impact of the surro unding environment on the conformation of this constrained peptidomime tic is discussed, The general structural features of the cyclic mimeti c are retained in both environments; however, the formation of a hydro phobic patch in the aqueous solvent is evident.