Synthesis, characterization, and folding behavior of beta-amino acid derived polyisocyanides

Abstract

Helical polymers of isocyanopeptides derived from beta-amino acids have been synthesized and their architectures have been studied in detail. Similar to their alpha-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 beta-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 beta-amino acid derived polyisocyanopeptides; this model is in contrast to the kinetically stable helical macromolecules that are formed upon polymerization of alpha-amino acid based isocyanopeptides.