Zouikri M, Vicherat A, Aubry A, Marraud M, Boussard G
LCPM, CNRS-URA-494, ENSIC-INPL, Nancy, France.
J Pept Res. 1998 Jul;52(1):19-26. doi: 10.1111/j.1399-3011.1998.tb00648.x.
Azaproline (AzPro) is an analogue of proline containing a nitrogen atom in place of the C(alpha)H group. AzPro has been introduced in various model peptides, and especially in the Boc-Ala-AzPro-Ala-NHiPr tripeptide. The structural consequence of that modification has been investigated in solution by using IR and 1H NMR, with reference to the cognate proline-containing peptide. Contrary to proline, which induces beta-folding of the Pro-Ala sequence, azaproline apparently favors betaVI-folding of the Ala-AzPro one with high occurrence. Opening of the AzPro pyrazolidine ring to get N-methylazaalanine fundamentally does not change the structural properties of the azatripeptide, but allows the existence of open conformers to an extent depending on the solvent.
氮杂脯氨酸（AzPro）是脯氨酸的类似物，其中的C（α）H基团被一个氮原子取代。AzPro已被引入各种模型肽中，特别是在Boc-Ala-AzPro-Ala-NHiPr三肽中。通过红外光谱（IR）和核磁共振氢谱（1H NMR），在溶液中研究了该修饰的结构后果，并以含同源脯氨酸的肽作为参考。与诱导Pro-Ala序列形成β折叠的脯氨酸相反，氮杂脯氨酸显然有利于Ala-AzPro序列以高发生率形成βVI折叠。将AzPro吡唑烷环打开得到N-甲基氮杂丙氨酸，从根本上来说并没有改变氮杂三肽的结构性质，但会在一定程度上允许开放构象的存在，这取决于溶剂。
