α-Peptide-Oligourea Chimeras: Stabilization of Short α-Helices by Non-Peptide Helical Foldamers
α-Peptide-Oligourea Chimeras: Stabilization of Short α-Helices by Non-Peptide Helical Foldamers
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DOI：
10.1002/anie.201500901
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发表时间：
2015-08-17
影响因子：
16.6
通讯作者：
Guichard, Gilles
中科院分区：
文献类型：
--
作者：
Fremaux, Juliette;Mauran, Laura;Guichard, Gilles
具有少于10个残基的短α-肽通常表现出低的成核稳定螺旋构象的倾向。虽然先前已经报道了稳定肽螺旋的各种策略，但尚未研究非肽螺旋折叠体在融合至短α-肽区段时稳定α-螺旋的能力。为此，对通过将脂肪族寡脲连接到α-肽的C-或N-末端而获得的一系列嵌合低聚物进行了结构研究。发现所有嵌合体都是完全螺旋的，其中少至2（或3）个脲单元足以在融合肽段中传播α-螺旋构象。α-肽与本文所述的寡脲的显著相容性，沿着该方法的简单性，突出了将天然和非肽主链连接作为进一步控制肽行为的手段的潜力。
Short alpha-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 alpha-helices when fused to short alpha-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 alpha-peptides are described. All chimeras were found to be fully helical, with as few as 2 (or 3) urea units sufficient to propagate an alpha-helical conformation in the fused peptide segment. The remarkable compatibility of alpha-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 apeptides.