Non‐classical Helices with cis Carbon–Carbon Double Bonds in the Backbone: Structural Features of α, γ‐Hybrid Peptide Foldamers. Issue 27 (6th June 2016)

• Record Type: Journal Article
• Authors: Ganesh Kumar, Mothukuri; Thombare, Varsha J.; Katariya, Mona M.; Veeresh, Kuruva; Raja, K. Muruga Poopathi; Gopi, Hosahudya N.
• Is Part Of: Angewandte Chemie international edition. Volume 55:Issue 27(2016)
• Page Start: 7847
• Page End: 7851
• Publication Date: 2016-06-06
• Subjects: foldamers -- non-natural amino acids -- peptide helices -- peptides -- X-ray crystallography; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201602861
• Languages: English
• ISSNs: 1433-7851

Abstract

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. Abstract : Do the twist : The design, synthesis, and solution and single‐crystal conformations of hybrid helices containing cis carbon–carbon double bonds in the backbone are presented. The results reveal that cis double bonds can be accommodated into the helix without deviation from the overall helical fold.