Structure–Property Relationship Study of N-(Hydroxy)Peptides for the Design of Self-Assembled Parallel β-Sheets | Zendy

Alexis D. Richaud | Zendy; Stéphane P. Roche | Zendy

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

Author(s) -

Alexis D. Richaud,

Stéphane P. Roche

Publication year - 2020

Publication title -

the journal of organic chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.2

H-Index - 228

eISSN - 1520-6904

pISSN - 0022-3263

DOI - 10.1021/acs.joc.0c01441

Subject(s) - chemistry , peptoid , hydrogen bond , peptide , self assembly , stereochemistry , beta sheet , cyclic peptide , glycine , protein secondary structure , foldamer , combinatorial chemistry , molecule , amino acid , organic chemistry , biochemistry

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 N -(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 N -(hydroxy)amides are outweighed by a network of strong interstrand hydrogen bonds.

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