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Issue 24, 2016
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Weak backbone CHO[double bond, length as m-dash]C and side chain tButBu London interactions help promote helix folding of achiral NtBu peptoids

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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[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

  • This article is part of the themed collection: Foldamers
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Publication details

The article was received on 14 Jan 2016, accepted on 17 Feb 2016 and first published on 17 Feb 2016


Article type: Communication
DOI: 10.1039/C6CC00375C
Citation: Chem. Commun., 2016,52, 4573-4576
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    Weak backbone CHO[double bond, length as m-dash]C and side chain tButBu London interactions help promote helix folding of achiral NtBu peptoids

    G. Angelici, N. Bhattacharjee, O. Roy, S. Faure, C. Didierjean, L. Jouffret, F. Jolibois, L. Perrin and C. Taillefumier, Chem. Commun., 2016, 52, 4573
    DOI: 10.1039/C6CC00375C

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