Constrained α/γ-peptides: A new stable extended structure in solution without any hydrogen bond and characterized by a four-fold symmetry

Article abstract of DOI:10.1039/c2cc16852a

Small α/γ-peptides alternating α-aminoisobutyric acid and cyclic γ-amino acid residues are described. NMR studies together with restrained simulated annealing revealed that an extended backbone conformation largely dominates in solution for as short as 4-residues long oligomers. This new fold type is devoid of any hydrogen bond and characterized by a four-fold symmetry.