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Non‐classical Helices with cis Carbon–Carbon Double Bonds in the Backbone: Structural Features of α,γ‐Hybrid Peptide Foldamers
Author(s) -
Ganesh Kumar Mothukuri,
Thombare Varsha J.,
Katariya Mona M.,
Veeresh Kuruva,
Raja K. Muruga Poopathi,
Gopi Hosahudya N.
Publication year - 2016
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.201602861
Subject(s) - chemistry , hydrogen bond , folding (dsp implementation) , carbon fibers , helix (gastropod) , reinforced carbon–carbon , crystallography , peptide , double bond , stereochemistry , amino acid , molecule , materials science , organic chemistry , biochemistry , ecology , composite number , snail , electrical engineering , composite material , engineering , biology
The impact of geometrically constrained cis α,β‐unsaturated γ‐amino acids on the folding of α,γ‐hybrid peptides was investigated. Structure analysis in single crystals and in solution revealed that the cis carbon–carbon double bonds can be accommodated into the 12‐helix without deviation from the overall helical conformation. The helical structures are stabilized by 4→1 hydrogen bonding in a similar manner to the 12‐helices of β‐peptides and the 3 10 helices of α‐peptides. These results show that functional cis carbon–carbon double bonds can be accommodated into the backbone of helical peptides.