New Class of Heterogeneous Helical Peptidomimetics

Org Lett. 2015 Jul 17;17(14):3524-7. doi: 10.1021/acs.orglett.5b01608. Epub 2015 Jul 8.


A new class of unnatural heterogeneous foldamers is reported to contain alternative α-amino acid and sulfono-γ-AA amino acid residues in a 1:1 repeat pattern. Two-dimensional NMR data show that two 1:1 α/sulfono-γ-AA peptides with diverse side chains form analogous right-handed helical structures in solution. The effects of sequence length, side chain, N-capping, and temperature on folding propensity were further investigated using circular dichroism and small-angle X-ray scattering.