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Structure-Property Relationship Study of N-(Hydroxy)Peptides for the Design of Self-Assembled Parallel ?-Sheets.

ABSTRACT: The design of novel and functional biomimetic foldamers remains a major challenge in creating mimics of native protein structures. Herein, we report the stabilization of a remarkably short ?-sheet by incorporating N-(hydroxy)glycine (Hyg) residues into the backbone of peptides. These peptide-peptoid hybrids form unique parallel ?-sheet structures by self-assembly upon hydrogenation. Our spectroscopic and crystallographic data suggest that the local conformational perturbations induced by N-(hydroxy)amides are outweighed by a network of strong interstrand hydrogen bonds.

SUBMITTER: Richaud AD

PROVIDER: S-EPMC7659681 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature

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Structure-Property Relationship Study of <i>N</i>-(Hydroxy)Peptides for the Design of Self-Assembled Parallel β-Sheets.

Richaud Alexis D AD Roche Stéphane P SP

The Journal of organic chemistry 20200917 19

The design of novel and functional biomimetic foldamers remains a major challenge in creating mimics of native protein structures. Herein, we report the stabilization of a remarkably short β-sheet by incorporating <i>N</i>-(hydroxy)glycine (Hyg) residues into the backbone of peptides. These peptide-peptoid hybrids form unique parallel β-sheet structures by self-assembly upon hydrogenation. Our spectroscopic and crystallographic data suggest that the local conformational perturbations induced by ...[more]

PMID: 32881524

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