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Polyisocyanides Derived from Tripeptides of Alanine
Author(s) -
Metselaar Gerald A.,
Adams P. J. Hans M.,
Nolte Roeland J. M.,
Cornelissen Jeroen J. L. M.,
Rowan Alan E.
Publication year - 2007
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.200600928
Subject(s) - tripeptide , hydrogen bond , dipeptide , alanine , side chain , steric effects , polymer , chemistry , circular dichroism , crystallography , stereochemistry , peptide , molecule , amino acid , organic chemistry , biochemistry
Helical polymers of isocyanotripeptides derived from alanine have been synthesized and their architectures studied in detail. The helical conformation of the polyisocyanotripeptides is stabilized by internal hydrogen‐bonding arrays between the tripeptide side chains. The possibility of extending the well‐defined hydrogen‐bonded array, from dipeptide to tripeptide side chains, depends strongly on the stereochemistry of the constituent alanine amino acids, as has been shown by circular dichroism and IR studies. In polymers containing a weaker hydrogen‐bonding array adjacent to the polymer backbone, due to steric interactions between the alanine methyl groups, a stronger second hydrogen‐bonding array was present between the peptide bonds furthest away from the main chain, which is probably a result of stretching/compression of the helical‐polymer conformation.