Doi M, Ishida T, Polese A, Formaggio F, Crisma M, Toniolo C, Broxterman Q B, Kamphuis J
Osaka University of Pharmaceutical Sciences, Japan.
Pept Res. 1995 Sep-Oct;8(5):294-7.
The first x-ray diffraction structure analysis of a C alpha-ethyl, C alpha-benzylglycine [(alpha Et)Phe]-containing peptide, N alpha-benzyloxycarbonyl-alpha-aminoisobutyryl-alpha-amino-isobutyr yl-(S)- C alpha-benzylglycyl-alpha-aminoisobutyric acid (methanol solvate), has been performed. In the crystal state the N alpha-protected tetrapeptide is folded in an incipient, left-handed 3(10)-helical structure. This finding confirms that the relationship between (alpha Et)Phe alpha-carbon chirality and screw sense of the helix that is formed is opposite to that exhibited by protein amino acids, including Phe.
已对一种含有Cα-乙基、Cα-苄基甘氨酸[（αEt）Phe]的肽，即Nα-苄氧羰基-α-氨基异丁酰基-α-氨基异丁酰基-（S）-Cα-苄基甘氨酰-α-氨基异丁酸（甲醇溶剂化物）进行了首次X射线衍射结构分析。在晶体状态下，Nα-保护的四肽折叠成一种初始的左手3(10)-螺旋结构。这一发现证实，（αEt）Phe的α-碳手性与所形成螺旋的螺旋方向之间的关系与包括Phe在内的蛋白质氨基酸所表现出的关系相反。
