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Non-classical helices with cis carbon-carbon double bonds in the backbone
Structural features of α, γ-hybrid peptide foldamers
Kumar, M. G., Thombare, V. J., Katariya, M. M., Veeresh, K., Raja, K. M. P., & Gopi, H. N. (2016). Non-classical helices with cis carbon-carbon double bonds in the backbone: Structural features of α, γ-hybrid peptide foldamers. Angewandte Chemie-International Edition, 55(27), 7847-7851. https://doi.org/10.1002/anie.201602861
The impact of geometrically constrained cis alpha, beta-unsaturated gamma-amino acids on the folding of alpha, gamma-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 beta-peptides and the 3(10) helices of alpha-peptides. These results show that functional cis carbon-carbon double bonds can be accommodated into the backbone of helical peptides.
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