A new generation of synthetic peptides, called foldamers, has emerged to provide bioinspired materials with unique structural properties. Foldamers, or oligomers that adopt specific secondary structures, provide endless possibilities in terms of their material and biological applications and tunability. When properly designed, foldamers can mimic the secondary structures of biologically active peptides with potentially higher affinity, greater specificity, and better physiological stability. Over the last two decades, this field has rapidly expanded from α-peptoids to linear and cyclic forms, as well as β- and γ-peptides. In particular, α-, β-, and γ-peptides adopt secondary structures, often helices, with greater stability than naturally occurring peptides. In a serendipitous discovery, we identified the unique sensitivity of cyclic β- and γ-peptoids towards a chiral environment. Cyclic, achiral β- and γ-peptoids were synthesized using SPPS, characterized by LC/MS, and their secondary structure was evaluated by FRET, CD, and NMR. When these achiral residues were used, the presence of one chiral amino acid induced organization of the backbone in a structure reminiscent of a helix. It is our strong contention that the molecular understanding of cyclic β- and γ-peptoids in foldamer chemistry is critical in determining their utility in material and biomedical applications.

Molecular investigation of cyclic β- and γ-peptoids

253rd National Meeting (2017)

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