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
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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.

催产素N -酰化三肽酰胺尾部构象的多功能性。三种C2 -主链修饰构象受限类似物的合成与晶体学表征。
本文对催产素N -酰化三肽酰胺尾部的三种类似物进行了合成、物理表征和分析表征,并通过x射线衍射进行了晶体状态结构分析,每一种类似物在2位上都含有环C - α, α -二取代甘氨酸。肽是Boc-L-Pro-Ac3c-Gly-NH2、Z-L-Pro-Ac5c-Gly-NH2和Z-L-Pro-Ac6c-Gly-NH2。前者在- l - pro - ac3c -序列上折叠成ii型β -转构象,后者形成两个连续的(ii型,i型)β -转构象。Ac5c-和ac6c -三肽是这种高度折叠结构组合的第一个例子,其位置类似于N -酰化- l - pro - l - leu - gly - nh2序列。
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