Nonpeptidic foldamers from amino acids: Synthesis and characterization of 1,3-substituted triazole oligomers

Nicholas G. Angelo; Paramjit S. Arora

doi:10.1021/ja056406z

Nonpeptidic foldamers from amino acids: Synthesis and characterization of 1,3-substituted triazole oligomers

Nicholas G. Angelo, Paramjit S. Arora

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English (US)
Pages (from-to)	17134-17135
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	127
Issue number	49
DOIs	https://doi.org/10.1021/ja056406z
State	Published - Dec 14 2005

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja056406z

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abstract = "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.",

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Nonpeptidic foldamers from amino acids: Synthesis and characterization of 1,3-substituted triazole oligomers

Abstract

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