Nonpeptidic foldamers from amino acids: Synthesis and characterization of 1,3-substituted triazole oligomers
Nonpeptidic foldamers from amino acids: Synthesis and characterization of 1,3-substituted triazole oligomers
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DOI：
10.1021/ja056406z
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发表时间：
2005-12-14
影响因子：
15
通讯作者：
Arora, PS
中科院分区：
文献类型：
--
作者：
Angelo, NG;Arora, PS
通过用1，2，3-三唑环交换酰胺键制备能够显示蛋白质样功能的非肽折叠体。这些三唑低聚物的整体构象主要由相邻环之间的偶极-偶极相互作用决定。溶液NMR研究表明，Z字形构象，这密切模仿的β-链结构，占主导地位的两个不同的四聚体。
Nonpeptidic foldamers capable of displaying protein-like functionality were prepared by swapping amide bonds with 1,2,3-triazole rings. The overall conformation of these triazole oligomers is largely dictated by dipole−dipole interactions between adjacent rings. Solution NMR studies suggest that a zigzag conformation, which closely mimics the β-strand structure, predominates in two different tetramers.