Synthesis, Characterization, and Folding Behavior of β‐Amino Acid Derived Polyisocyanides

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Abstract
Helical polymers of isocyanopeptides derived from β-amino acids have been synthesized and their architectures have been studied in detail. Similar to their α-amino acid analogues, the helical conformation in these macromolecules is stabilized by internal hydrogen-bonding arrays along the polymeric backbone. Unexpectedly, the flexibility of the β-peptide side arms results in a rearrangement of the initial macromolecular architecture, leading to a more stable helical structure possessing a better defined hydrogen-bonding pattern, as was concluded from IR and temperature-dependent circular dichroism studies. Based on these results we propose a dynamic helical model for the β-amino acid derived polyisocyanopeptides; this model is in contrast to the kinetically stable helical macromolecules that are formed upon polymerization of α-amino acid based isocyanopeptides.