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- Title
Non-classical Helices with cis Carbon-Carbon Double Bonds in the Backbone: Structural Features of α,γ-Hybrid Peptide Foldamers.
- Authors
Ganesh Kumar, Mothukuri; Thombare, Varsha J.; Katariya, Mona M.; Veeresh, Kuruva; Raja, K. Muruga Poopathi; Gopi, Hosahudya N.
- Abstract
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 310 helices of α-peptides. These results show that functional cis carbon-carbon double bonds can be accommodated into the backbone of helical peptides.
- Subjects
PEPTIDES; CARBON-carbon bonds; AMINO acids; SINGLE crystals; HYDROGEN bonding
- Publication
Angewandte Chemie, 2016, Vol 128, Issue 27, p7978
- ISSN
0044-8249
- Publication type
Article
- DOI
10.1002/ange.201602861