文摘
A new class of unnatural heterogeneous foldamers is reported to contain alternative 伪-amino acid and sulfono-纬-AA amino acid residues in a 1:1 repeat pattern. Two-dimensional NMR data show that two 1:1 伪/sulfono-纬-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.