Crystalline Cyclophane-Protein Cage Frameworks

ACS Nano. 2018 Aug 28;12(8):8029-8036. doi: 10.1021/acsnano.8b02856. Epub 2018 Jul 20.


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.

Keywords: crystal; cyclophane; electrostatic binding; pillararene; protein cage; self-assembly.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Ethers, Cyclic / chemistry*
  • Ferritins / chemistry*
  • Metal-Organic Frameworks / chemistry*
  • Models, Molecular
  • Particle Size
  • Porosity
  • Surface Properties


  • Ethers, Cyclic
  • Metal-Organic Frameworks
  • Ferritins