Journal article

Non-classical Helices with cis Carbon-Carbon Double Bonds in the Backbone: Structural Features of alpha, gamma-Hybrid Peptide Foldamers

Mothukuri Ganesh Kumar, Varsha J Thombare, Mona M Katariya, Kuruva Veeresh, K Muruga Poopathi Raja, Hosahudya N Gopi

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | WILEY-V C H VERLAG GMBH | Published : 2016

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.