Uniformly Nucleobase-Functionalized β-Peptide Helices: Watson–Crick Pairing or Nonspecific Aggregation
Uniformly Nucleobase-Functionalized β-Peptide Helices: Watson–Crick Pairing or Nonspecific Aggregation
复制标题
均匀核碱基功能化的 β-肽螺旋：Watson-Crick 配对或非特异性聚集
DOI：
10.1002/ejoc.200700444
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发表时间：
2007
影响因子：
2.8
通讯作者：
U. Diederichsen
中科院分区：
文献类型：
--
作者：
A. Weiss;U. Diederichsen
螺旋的组织和结构是蛋白质三级结构折叠的基础。因此，稳定的β-肽螺旋被用作选择性组织二级结构的模型。碱基已经被确定为识别元件，以反平行的方向组织两个β-肽螺旋。对用一种类型的碱基统一官能化的β-肽螺旋的研究为进一步了解线性和非常刚性的螺旋主干拓扑中的特定相互作用的识别模式和要求提供了进一步的见解。一旦Watson-Crick配对被允许，基于碱基对识别的特定螺旋相互作用就占主导地位。如果氢键供体/受体模式禁止Watson-Crick几何构型，则基于芳香族相互作用或非特异性氢键网络，发现了相当稳定的非特异性相互作用。酪氨酸侧链也证实了后一种聚集(Wiley-VCH Verlag GmbH&Co.KGaA，69451 Weinheim，德国，2005年)。
The organization and architecture of helices is fundamental in folding of protein tertiary structures. Therefore, stable β-peptide helices are used as models for the selective organization of secondary structures. Nucleobases are already established as recognition elements to organize two β-peptide helices in antiparallel orientation. The investigation of β-peptide helices uniformly functionalized with one type of nucleobases provided further insight in the recognition mode and requirements for specific interaction within the linear and very rigid helical backbone topology. Specific helix interaction based on base pair recognition is predominant as soon as Watson–Crick pairing is allowed. If the hydrogen bonding donor/acceptor pattern prohibits the Watson–Crick geometry, a quite stable nonspecific interaction was found based on aromatic interactions or on a nonspecific hydrogen bonding network. The latter aggregation was also confirmed with tyrosine side chains.(© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2005)
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