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

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

206 Scopus citations

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
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 - 14 Dec 2005
Externally published	Yes

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

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.",

author = "Angelo, \{Nicholas G.\} and Arora, \{Paramjit S.\}",

year = "2005",

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AU - Angelo, Nicholas G.

AU - Arora, Paramjit S.

PY - 2005/12/14

Y1 - 2005/12/14

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/29044447377

U2 - 10.1021/ja056406z

DO - 10.1021/ja056406z

M3 - Article

C2 - 16332031

AN - SCOPUS:29044447377

SN - 0002-7863

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EP - 17135

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 49

ER -

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

Abstract

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