Flaws in foldamers: conformational uniformity and signal decay in achiral helical peptide oligomers.

ABSTRACT: Although foldamers, by definition, are extended molecular structures with a well-defined conformation, minor conformers must be populated at least to some extent in solution. We present a quantitative analysis of these minor conformers for a series of helical oligomers built from achiral but helicogenic α-amino acids. By measuring the chain length dependence or chain position dependence of NMR or CD quantities that measure screw-sense preference in a helical oligomer, we quantify values for the decay constant of a conformational signal as it passes through the molecular structure. This conformational signal is a perturbation of the racemic mixture of M and P helices that such oligomers typically adopt by the inclusion of an N or C terminal chiral inducer. We show that decay c

SUBMITTER: Le Bailly BAF 

PROVIDER: S-EPMC5645781 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature