Crystalline Cyclophane–Protein Cage Frameworks

Research output: Contribution to journalArticleScientificpeer-review

Researchers

Research units

  • University of Windsor
  • Oakland University
  • University of Applied Sciences and Arts of Southern Switzerland

Abstract

Cyclophanes are macrocyclic supramolecular hosts famous for their ability to bind atomic or molecular guests via noncovalent interactions within their well-defined cavities. In a similar way, porous crystalline networks, such as metal–organic frameworks, can create microenvironments that enable controlled guest binding in the solid state. Both types of materials often consist of synthetic components, and they have been developed within separate research fields. Moreover, the use of biomolecules as their structural units has remained elusive. Here, we have synthesized a library of organic cyclophanes and studied their electrostatic self-assembly with biological metal-binding protein cages (ferritins) into ordered structures. We show that cationic pillar[5]arenes and ferritin cages form biohybrid cocrystals with an open protein network structure. Our cyclophane–protein cage frameworks bridge the gap between molecular frameworks and colloidal nanoparticle crystals and combine the versatility of synthetic supramolecular hosts with the highly selective recognition properties of biomolecules. Such host–guest materials are interesting for porous material applications, including water remediation and heterogeneous catalysis.

Details

Original languageEnglish
Article number8b02856
Pages (from-to)8029-8036
JournalACS Nano
Volume12
Issue number8
Publication statusPublished - 13 Jul 2018
MoE publication typeA1 Journal article-refereed

    Research areas

  • protein cage, cyclophane, pillararene, crystal, self-assembly, electrostatic binding

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