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Updated: Jul 7, 2026
09:22
Self-assembling Morphologies Obtained from Helical Polycarbodiimide Copolymers and Their Triazole Derivatives
Published on: February 7, 2017
Naphthyridine-based helical foldamers and macrocycles: synthesis, cation binding, and supramolecular assemblies
Anne Petitjean1, Louis A Cuccia, Marc Schmutz
1Laboratoire de Chimie Supramoléculaire, Institut de Science et d'Ingénierie Supramoléculaires, Université Louis Pasteur, 8 Allée Gaspard Monge, BP 70028, 67083 Strasbourg Cedex, France.
The Journal of Organic Chemistry
|March 5, 2008
Summary
This study introduces novel foldamers and macrocycles that self-assemble into helical structures. Ion binding influences their aggregation and assembly, offering new possibilities for designing complex molecular systems.
Area of Science:
- Supramolecular Chemistry
- Organic Chemistry
- Materials Science
Background:
- Understanding molecular chain conformation is crucial for biological and artificial systems.
- Artificial folding codons guide the formation of helices, strands, and loops in foldamers.
Purpose of the Study:
- To synthesize and investigate foldamers and macrocycles based on 1,8-naphthyridine and pyrimidine units.
- To explore the impact of ionic guest binding on the supramolecular assembly and external interactions of these systems.
Main Methods:
- Synthesis of novel foldamers and macrocycles.
- Investigation of ion-binding effects on molecular conformation and aggregation.
- Characterization of one-turn, two-turn helices, and macrocycles.
Main Results:
- Foldamers and macrocycles accommodate ionic substrates within a cylindrical cavity.
- Ion binding influences external interactions, promoting fibril formation with alkali cations.
- Polyammonium substrates modulate helix assembly length and oligomer rigidity.
Conclusions:
- A model for ion-controlled supramolecular assembly of these systems is proposed.
- These controlled scaffolds show promise for designing complex molecular systems.
- The study highlights the external effects of internal guest binding in large oligomers.
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