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Structural Diversity of Peptoids: Tube-Like Structures of Macrocycles

Herlan, Claudine Nicole; Sommer, Katharina; Weis, Patrick; Nieger, Martin; Bräse, Stefan

Abstract:
Peptoids, or poly-N-substituted glycines, are characterised by broad structural diversity. Compared to peptides, they are less restricted in rotation and lack backbone-derived H bonding. Nevertheless, certain side chains force the peptoid backbone into distinct conformations. Designable secondary structures like helices or nanosheets arise from this knowledge. Herein, we report the copper-catalysed alkyne-azide cycloaddition (CuAAC) of macrocycles to form innovative tube-like tricyclic peptoids, giving access to host–guest chemistry or storage applications. Different linker systems make the single tubes tuneable in size and enable modifications within the gap. An azobenzene linker, which is reversibly switchable in conformation, was successfully incorporated and allowed for light-triggered changes of the entire tricyclic structure.

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Verlagsausgabe §
DOI: 10.5445/IR/1000129359
Veröffentlicht am 05.02.2021
Cover der Publikation
Zugehörige Institution(en) am KIT Institut für Organische Chemie (IOC)
Institut für Physikalische Chemie (IPC)
Institut für Biologische und Chemische Systeme (IBCS)
Publikationstyp Zeitschriftenaufsatz
Publikationsdatum 31.12.2020
Sprache Englisch
Identifikator ISSN: 1420-3049
KITopen-ID: 1000129359
HGF-Programm 47.01.01 (POF III, LK 01) Biol.Netzwerke u.Synth.Regulat. ITG+ITC
Erschienen in Molecules
Verlag MDPI
Band 26
Heft 1
Seiten Art.-Nr.: 150
Schlagwörter peptidomimetics; tricyclic peptoids; CuAAC; foldamers
Nachgewiesen in Scopus
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Web of Science
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