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Turning Peptide Sequences into Ribbon Foldamers by a Straightforward Multicyclization Reaction
Author(s) -
Martin Vincent,
Legrand Baptiste,
Vezenkov Lubomir L.,
Berthet Mathéo,
Subra Gilles,
Calmès Monique,
Bantignies JeanLouis,
Martinez Jean,
Amblard Muriel
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201506955
Subject(s) - peptide , sequence (biology) , ribbon , chemistry , functional diversity , combinatorial chemistry , peptide sequence , molecule , peptidomimetic , amino acid , protein secondary structure , nanotechnology , stereochemistry , materials science , biochemistry , biology , organic chemistry , ecology , gene , composite material
The conformational control of molecular scaffolds allows the display of functional groups in defined spatial arrangement. This is of considerable interest for developing fundamental and applied systems in both the fields of biology and material sciences. Peptides afford a large diversity of functional groups, and peptide synthetic routes are very attractive and accessible. However, most short peptides do not possess well‐defined secondary structures. Herein, we developed a simple strategy for converting peptide sequences into structured γ‐lactam‐containing oligomers while keeping the amino acids side chain diversity. We showed the propensity of these molecules to adopt ribbon‐like secondary structures. The periodic distribution of the functional groups on both sides of the ribbon plane is encoded by the initial peptide sequence.