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New Class of Heterogeneous Helical Peptidomimetics
- Wu, Haifan, Qiao, Qiao, Teng, Peng, Hu, Yaogang, Antoniadis, Dimitrios, Zuo, Xiaobing, Cai, Jianfeng
- Organic letters 2015 v.17 no.14 pp. 3524-3527
- X-radiation, amino acids, chemical reactions, chemical structure, circular dichroism spectroscopy, nuclear magnetic resonance spectroscopy, organic compounds, peptides, temperature
- 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.