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Surprisingly Stable Helical Conformations in α/β‐Peptides by Incorporation of cis ‐β‐Aminocyclopropane Carboxylic Acids
Author(s) -
De Pol Silvia,
Zorn Chiara,
Klein Christian D.,
Zerbe Oliver,
Reiser Oliver
Publication year - 2004
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200352267
Subject(s) - chemistry , alanine , stereochemistry , helix (gastropod) , amino acid , biochemistry , biology , ecology , snail
With as few as seven residues , acyclic α/β‐peptides, which consist of alternating units of ( L )‐alanine and of cis ‐β‐aminocyclopropanecarboxylic acids ( cis ‐β‐ACCs, see structure), form stable 3 13 ‐helix turns in solution. The configuration of the cis ‐β‐ACCs was found to be crucial for the helical structure of this new class of foldamers.
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