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⋯OC hydrogen bonding along the peptoid backbone and London interaction between tBu⋯tBu side-chains.

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

Bhattacharjee, N.
Writing – Review & Editing
;
2016

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⋯OC hydrogen bonding along the peptoid backbone and London interaction between tBu⋯tBu side-chains.
Crystallography, X-Ray; Magnetic Resonance Spectroscopy; Models, Molecular; Peptides; Proton Magnetic Resonance Spectroscopy; Stereoisomerism; Protein Folding; Catalysis; Electronic, Optical and Magnetic Materials; Ceramics and Composites; Chemistry (all); Surfaces, Coatings and Films; 2506; Materials Chemistry2506 Metals and Alloys
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11384/73160
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