Crisma M, Bonora G M, Toniolo C, Barone V, Benedetti E, Di Blasio B, Pavone V, Pedone C, Santini A, Fraternali F
Department of Organic Chemistry, University of Padua, Italy.
Int J Biol Macromol. 1989 Dec;11(6):345-52. doi: 10.1016/0141-8130(89)90006-8.
Conformational energy computations on the 1-aminocyclopropane-1-carboxylic acid mono-, di-, and tripeptide amides, Ac-(Ac3c)n-NHMe (n = 1-3), indicate that this C alpha, alpha-dialkylated, cyclic alpha-amino acid residue is conformally restricted and that type-I(I') beta-bends and distorted 3(10)-helices are particularly stable conformations for the di- and tripeptide amides, respectively. The results of the theoretical analysis are in agreement with those obtained in an i.r. absorption and 1H n.m.r. investigation in chloroform solution of Ac3c-rich tri- and tetrapeptide esters. A comparison is also made with the conclusions extracted from our previous work on peptides rich in Aib (alpha-aminoisobutyric acid), Ac5c (1-aminocyclopentane-1-carboxylic acid), and Ac6c (1-aminocyclohexane-1-carboxylic acid).
对1-氨基环丙烷-1-羧酸单肽、二肽和三肽酰胺Ac-(Ac3c)n-NHMe（n = 1 - 3）进行的构象能计算表明，这种α,α-二烷基化的环状α-氨基酸残基在构象上受到限制，并且I型（I'型）β-转角和扭曲的3(10)-螺旋分别是二肽酰胺和三肽酰胺特别稳定的构象。理论分析结果与在富含Ac3c的三肽和四肽酯的氯仿溶液中进行的红外吸收和1H核磁共振研究结果一致。还与我们之前关于富含Aib（α-氨基异丁酸）、Ac5c（1-氨基环戊烷-1-羧酸）和Ac6c（1-氨基环己烷-1-羧酸）的肽的研究得出的结论进行了比较。
