Sculpting the β-peptide foldamer H12 helix via a designed side-chain shape

摘要

The long-range side-chain repulsion between the (1R,2R,3R,5R)-2-amino-6,6-dimethyl-bicyclo[3.1.1]-heptane-3-carboxylic acid (trans-ABHC) residues stabilize the H12 helix in p-peptide oligomers.rnSynthetic oligomers with distinct conformational preferences (foldamers) are highly intriguing compounds at the interface of covalent and supramolecular (noncovalent) chemistry. Among foldamers based on remote intrastrand interactions, peptides containing β-amino acid residues are probably the most thoroughly studied systems. Their versatile secondary structure patterns and the side-chain controllable conformational preferences are attracting increasing interest. β-Peptide oligomers with designed molecular interaction fields have gained a number of biological applications, such as rationally designed antiviral H12 helices.