Conformational versatility of the N alpha-acylated tripeptide amide tail of oxytocin. Synthesis and crystallographic characterization of three C2 alpha-backbone modified, conformationally restricted analogues.

N Fabiano, G Valle, M Crisma, C Toniolo, M Saviano, A Lombardi, C Isernia, V Pavone, B Di Blasio, C Pedone

Index: Int. J. Pept. Protein Res. 42 , 459, (1993)

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Abstract

The synthesis, physical and analytical characterization, and crystal-state structural analysis by X-ray diffraction of three analogues of the N alpha-acylated tripeptide amide tail of oxytocin, each containing a cyclic C alpha, alpha-disubstituted glycine at position 2, have been performed. The peptides are Boc-L-Pro-Ac3c-Gly-NH2, Z-L-Pro-Ac5c-Gly-NH2 and Z-L-Pro-Ac6c-Gly-NH2. While the former is folded in a type-II beta-turn conformation at the -L-Pro-Ac3c- sequence, the two latter tripeptides form two consecutive (type-II, type-I') beta-turns. The Ac5c- and Ac6c-tripeptides are the first examples of such a highly folded structural combination in a position-2 analogue of the N alpha-acylated -L-Pro-L-Leu-Gly-NH2 sequence.