| Literature DB >> 26153619 |
Haifan Wu1, Qiao Qiao1, Peng Teng1, Yaogang Hu1, Dimitrios Antoniadis1, Xiaobing Zuo2, Jianfeng Cai1.
Abstract
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.Entities:
Year: 2015 PMID: 26153619 DOI: 10.1021/acs.orglett.5b01608
Source DB: PubMed Journal: Org Lett ISSN: 1523-7052 Impact factor: 6.005