Univ. Bordeaux, CBMN, UMR 5248, Institut Européen de Chimie et Biologie (IECB), 2 rue Robert Escarpit, 33607 Pessac (France).
CNRS, CBMN, UMR 5248, 33600 Pessac (France).
Angew Chem Int Ed Engl. 2015 Aug 17;54(34):9816-20. doi: 10.1002/anie.201500901. Epub 2015 Jul 1.
Short α-peptides with less than 10 residues generally display a low propensity to nucleate stable helical conformations. While various strategies to stabilize peptide helices have been previously reported, the ability of non-peptide helical foldamers to stabilize α-helices when fused to short α-peptide segments has not been investigated. Towards this end, structural investigations into a series of chimeric oligomers obtained by joining aliphatic oligoureas to the C- or N-termini of α-peptides are described. All chimeras were found to be fully helical, with as few as 2 (or 3) urea units sufficient to propagate an α-helical conformation in the fused peptide segment. The remarkable compatibility of α-peptides with oligoureas described here, along with the simplicity of the approach, highlights the potential of interfacing natural and non-peptide backbones as a means to further control the behavior of α-peptides.
短 α-肽通常具有小于 10 个残基，其形成稳定螺旋构象的倾向较低。虽然以前已经报道了各种稳定肽螺旋的策略，但非肽螺旋构象稳定体与短 α-肽片段融合时稳定 α-螺旋的能力尚未得到研究。为此，描述了通过将脂族寡脲连接到 α-肽的 C-或 N-末端获得的一系列嵌合低聚物的结构研究。发现所有嵌合体都是完全螺旋的，在融合的肽段中，仅 2（或 3）个脲基单元就足以传播 α-螺旋构象。这里描述的 α-肽与寡脲的惊人兼容性，以及该方法的简单性，突出了界面连接天然和非肽骨架作为进一步控制 α-肽行为的手段的潜力。
