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 CHâ¯OC hydrogen bonding along the peptoid backbone and London interaction between tBuâ¯tBu side-chains.
Weak backbone CHâ¯OC and side chain tBuâ¯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 CHâ¯OC hydrogen bonding along the peptoid backbone and London interaction between tBuâ¯tBu side-chains.File in questo prodotto:
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