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Artificial β‐Double Helices from Achiral γ‐Peptides
Author(s) -
Misra Rajkumar,
Dey Sanjit,
Reja Rahi M.,
Gopi Hosahudya N.
Publication year - 2018
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.201711124
Subject(s) - chemistry , peptide , double bond , stereochemistry , double stranded , helix (gastropod) , nuclear magnetic resonance spectroscopy , cyclic peptide , crystallography , amide , dna , biochemistry , organic chemistry , biology , ecology , snail
Double helices are not common in polypeptides and proteins except in the peptide antibiotic gramicidin A and analogous l,d ‐peptides. In contrast to natural polypeptides, remarkable β‐double‐helical structures from achiral γ‐peptides built from α,β‐unsaturated γ‐amino acids have been observed. The crystal structures suggest that they adopted parallel β‐double helical structures and these structures are stabilized by the interstrand backbone amide H‐bonds. Furthermore, both NMR spectroscopy and fluorescence studies support the existence of double‐helical conformations in solution. Although a variety of folded architectures featuring distinct H‐bonds have been discovered from the β‐ and γ‐peptide foldamers, this is the first report to show that achiral γ‐peptides can spontaneously intertwine into β‐double helical structures.