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Synthesis, Characterization, and Folding Behavior of β‐Amino Acid Derived Polyisocyanides
Author(s) -
Wezenberg Sander J.,
Metselaar Gerald A.,
Rowan Alan E.,
Cornelissen Jeroen J. L. M.,
Seebach Dieter,
Nolte Roeland J. M.
Publication year - 2006
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200501042
Subject(s) - macromolecule , folding (dsp implementation) , amino acid , circular dichroism , hydrogen bond , polymer , polymerization , chemistry , flexibility (engineering) , peptide , crystallography , stereochemistry , polymer chemistry , molecule , organic chemistry , biochemistry , statistics , mathematics , electrical engineering , engineering
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.