Synthesis, characterization, and folding behavior of beta-amino acid derived polyisocyanides.
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.
Wezenberg
Sander J
SJ
Institute for Molecules and Materials, Radboud University Nijmegen, Toernooiveld 1, 6525 ED, Nijmegen, The Netherlands.
Metselaar
Gerald A
GA
Rowan
Alan E
AE
Cornelissen
Jeroen J L M
JJ
Seebach
Dieter
D
Nolte
Roeland J M
RJ
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D002942:Circular Dichroism; D003486:Cyanides / Q000737:chemistry*; D006860:Hydrogen Bonding; D007700:Kinetics; D008956:Models, Chemical; D009842:Oligopeptides / Q000138:chemical synthesis*; D017510:Protein Folding; D017433:Protein Structure, Secondary
D000596:Amino Acids; D003486:Cyanides; D009842:Oligopeptides