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Abstract | Cited by

The synthesis of all-cis amide (NtBu)-glycine oligomers up to 15 residues long by a blockwise coupling approach is reported. The structure and dynamical behavior of these peptoids have been studied by X-ray crystallography, NMR and molecular modeling. Analyses reveal that the folding of these oligomers is driven by weak CH⋯O[double bond, length as m-dash]C hydrogen bonding along the peptoid backbone and London interaction between tBu⋯tBu side-chains.

Graphical abstract: Weak backbone CH⋯O [[double bond, length as m-dash]] C and side chain tBu⋯tBu London interactions help promote helix folding of achiral NtBu peptoids

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