Unnatural oligomers that fold into discrete helical structures may have promise for theinvestigation, understanding, and mimicry of protein structures and functions. Herein we reporta new class of unnatural heterogeneous foldamer backbone, which contains sulfono-?-AA and a-amino acid residues in a 1:1 repeat pattern. This type of oligomers projects same number of sidechains as a-peptides of same length. Two-dimensional NMR data shows that the 1:1 a/sulfono-?-AA peptide forms a well-defined right-handed helical structure in solution. It suggests thata/sulfono-?-AA heterogeneous peptides may represent a new class of unnatural foldamer withdiscrete functions in the near future.

An a/sulfono-?-AA heterogeneous helical peptide

247th National Meeting (2014)

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