Peptides of aminoxy acids as foldamers

Abstract

This Feature Article summarizes our efforts in developing a new family of foldamers from α-, β- and γ-aminoxy acids. From a series of conformational studies, we demonstrate that peptides consisting of aminoxy acids adopt several well-defined secondary structures, such as α N–O turns (which feature an eight-membered-ring hydrogen bond), β N–O turns (a nine-membered-ring hydrogen bond), γ N–O turns (a ten-membered-ring hydrogen bond), 1.8₈ helices (consecutive homochiral α N–O turns), 7/8 helices (alternating α N–O turns and γ-turns), 1.7₉ helices (consecutive β N–O turns), reverse turns (consecutive heterochiral α N–O turns) and sheet-like structures.