Open AccessStructure–Property Relationship Study of N-(Hydroxy)Peptides for the Design of Self-Assembled Parallel β-Sheets
Author(s) -
Alexis Richaud,
Stéphane Roche
Publication year - 2020
Publication title -
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) - peptoid , hydrogen bond , chemistry , peptide , beta sheet , self assembly , stereochemistry , glycine , protein secondary structure , combinatorial chemistry , amino acid , molecule , 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.