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Weak backbone CH⋯OC and side chain tBu⋯tBu London interactions help promote helix folding of achiral NtBu peptoids

Author:
Angelici, G., Bhattacharjee, N., Roy, O., Faure, S., Didierjean, C., Jouffret, L., Jolibois, F., Perrin, L., Taillefumier, C.
Source:
Chemical communications 2016 v.52 no.24 pp. 4573-4576
ISSN:
1364-548X
Subject:
N-substituted glycines, X-ray diffraction, chemical compounds, chemical reactions, hydrogen bonding, molecular models, nuclear magnetic resonance spectroscopy
Abstract:
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C hydrogen bonding along the peptoid backbone and London interaction between tBu⋯tBu side-chains.
Agid:
6387161