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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Bibliographic Details
Published inJournal of the American Chemical Society Vol. 128; no. (14) ; 02, 2006
Main Authors Schmitt, Margaret A., Choi, SooHyuk, Guzei, Ilia A., Gellman, Samuel H.
Format Journal Article
LanguageEnglish
Published United States 03.10.2008
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ISSN0002-7863
1520-5126
DOI10.1021/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.
Bibliography:USDOE
ISSN:0002-7863
1520-5126
DOI:10.1021/ja060281w