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Fine Tuning of β‐Peptide Foldamers: a Single Atom Replacement Holds Back the Switch from an 8‐Helix to a 12‐Helix
Author(s) -
AltmayerHenzien Amandine,
Declerck Valérie,
Farjon Jonathan,
Merlet Denis,
Guillot Régis,
Aitken David J.
Publication year - 2015
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201504126
Subject(s) - helix (gastropod) , foldamer , oligomer , chemistry , triple helix , peptide , turn (biochemistry) , stereochemistry , crystallography , biochemistry , polymer chemistry , ecology , snail , biology
Cyclic homologated amino acids are important building blocks for the construction of helical foldamers. N ‐aminoazetidine‐2‐carboxylic acid (AAzC), an aza analogue of trans‐ 2‐aminocyclobutanecarboxylic acid ( t ACBC), displays a strong hydrazino turn conformational feature, which is proposed to act as an 8‐helix primer. t ACBC oligomers bearing a single N‐terminal AAzC residue were studied to evaluate the ability of AAzC to induce and support an 8‐helix along the oligopeptide length. While t ACBC homooligomers assume a dominant 12‐helix conformation, the aza‐primed oligomers preferentially adopt a stabilized 8‐helix conformation for an oligomer length up to 6 residues. The (formal) single‐atom exchange at the N terminus of a t ACBC oligomer thus contributes to the sustainability of the 8‐helix, which resists the switch to a 12‐helix. This effect illustrates atomic‐level programmable design for fine tuning of peptide foldamer architectures.