Discrete heterogeneous quaternary structure formed by α/β-peptide foldamers and α-peptides
Discrete heterogeneous quaternary structure formed by α/β-peptide foldamers and α-peptides
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DOI：
10.1021/ja071203r
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发表时间：
2007-05-23
影响因子：
15
通讯作者：
Gellman, Samuel H.
中科院分区：
文献类型：
--
作者：
Price, Joshua L.;Horne, W. Seth;Gellman, Samuel H.
采用可预测二级结构的非天然低聚物的发展导致了人们对扩大折叠分子构象谱以包括离散的、协同折叠的三级和四级结构的兴趣的增加。在这里，我们报道了非均相四元结构的第一个例子：稳定的四聚体螺旋束，包含α-肽和α/β-肽折叠体。结果表明，螺旋束核心的疏水相互作用有助于组装的稳定性，环β-氨基酸残基也是如此。这些观察表明，折叠良好的三级或四级结构中的二级结构元素不需要具有相同的主干成分。我们的发现强调了这样一种前景，即不同的Folamer和α-肽亚单位的组合可能导致折叠和/或组装行为，这让人想起复杂蛋白质功能所必需的行为。
The development of unnatural oligomers that adopt predictable secondary structures has led to increased interest in expanding the conformational repertoire of foldamers to include discrete, cooperatively folded tertiary and quaternary structures. Here we report the first examples of heterogeneous quaternary structure: stable tetrameric helix bundles incorporating both alpha-peptides and alpha/beta-peptide foldamers. The results suggest that hydrophobic interactions in the core of the helix bundle contribute to the stability of the assembly, as do cyclic beta-amino acid residues within the alpha/beta-peptide. These observations demonstrate that secondary structural elements in well-folded tertiary or quaternary structures need not have the same backbone composition. Our findings highlight the prospect that diverse combinations of foldamer and alpha-peptide subunits could lead to folding and/or assembly behavior reminiscent of that necessary for complex protein function.