Toniolo C, Crisma M, Bonora G M, Klajc B, Lelj F, Grimaldi P, Rosa A, Polinelli S, Boesten W H, Meijer E M
C.N.R., Department of Organic Chemistry, University of Padova, Italy.
Int J Pept Protein Res. 1991 Sep;38(3):242-52. doi: 10.1111/j.1399-3011.1991.tb01435.x.
Conformational energy computations on Ac-L-(alpha Me)Val-NHMe indicate that turns and right-handed helical structures are particularly stable conformations for this chiral C alpha-methyl, C alpha-alkylglycyl residue. We have synthesized and characterized a variety of L-(alpha Me)Val derivatives and peptides (to the pentamer level). The results of the solution conformational analysis, performed using infrared absorption, 1H nuclear magnetic resonance, and circular dichroism, are in general agreement with those obtained from the theoretical investigation, in the sense that the L-(alpha Me)Val residue turns out to be a strong beta-turn and right-handed helix former. A comparison is also made with the conclusions extracted from published work on peptides rich in other C alpha-methyl, C alpha-alkylglycyl residues.
对乙酰基-L-(α-甲基)缬氨酸甲酯进行的构象能量计算表明，对于这种手性α-甲基、α-烷基甘氨酰残基，转角和右手螺旋结构是特别稳定的构象。我们已经合成并表征了多种L-(α-甲基)缬氨酸衍生物和肽（直至五聚体水平）。使用红外吸收、1H核磁共振和圆二色性进行的溶液构象分析结果，在L-(α-甲基)缬氨酸残基是强β-转角和右手螺旋形成者这一点上，总体上与理论研究结果一致。还与从关于富含其他α-甲基、α-烷基甘氨酰残基的肽的已发表工作中得出的结论进行了比较。
