New Helical Foldamers: Heterogeneous Backbones with 1:2 and 2:1 [alpha]:[superscript beta]-Amino Acid Residue Patterns
Foldamers, oligomers with strong folding propensities, are subjects of growing interest because such compounds offer unique scaffolds for the development of molecular function. We report two new foldamer classes, oligopeptides with regular 1:2 or 2:1 patterns of {alpha}- and {beta}-amino acid residu...
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Published in | Journal of the American Chemical Society Vol. 128; no. (14) ; 02, 2006 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
United States
03.10.2008
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Subjects | |
Online Access | Get full text |
ISSN | 0002-7863 1520-5126 |
DOI | 10.1021/ja060281w |
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Summary: | Foldamers, oligomers with strong folding propensities, are subjects of growing interest because such compounds offer unique scaffolds for the development of molecular function. We report two new foldamer classes, oligopeptides with regular 1:2 or 2:1 patterns of {alpha}- and {beta}-amino acid residues. Two distinct helical conformations are detected via 2D NMR in methanol for each backbone. One of the helices for each backbone is characterized via X-ray crystallography. |
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Bibliography: | USDOE |
ISSN: | 0002-7863 1520-5126 |
DOI: | 10.1021/ja060281w |