Colloidal Assembly of Hierarchically Structured Porous Supraparticles from Flower-Shaped Protein-Inorganic Hybrid Nanoparticles

ACS Nano. 2016 Sep 27;10(9):8271-80. doi: 10.1021/acsnano.6b01003. Epub 2016 Aug 23.


Mimicry of biomineralization is an attractive strategy to fabricate nanostructured hybrid materials. While biomineralization involves processes that organize hybrid clusters into complex structures with hierarchy, arrangement of artificial components in biomimetic approaches has been challenging. Here, we demonstrate self-assembly of hierarchically structured porous supraparticles from protein-inorganic hybrid flower-shaped (FS) nanoparticle building blocks. In our strategy, the FS nanoparticles self-assemble via high valency interactions in combination with interfacial adsorption and compression. The flower-like shape directed robust assembly of the FS nanoparticles into chain-like clusters in solution, which were further assembled into spherical supraparticles during rotation of FS nanoparticle solution. Continuously expanding and contracting the air-water interface during rotation catalyzed assembly of FS nanoparticle clusters, indicating that adsorption and compression of the building blocks at the interface were critical. The resulting supraparticles contain hierarchical pores which are translated from the structural characteristics of individual FS nanoparticle building blocks. The protein-inorganic supraparticles are protein-compatible, have large surface area, and provide specific affinity recognition for robust protein immobilization. A variety of functional proteins could be immobilized to the porous supraparticles, making it a general platform that could provide benefits for many applications.

Keywords: colloidal assembly; hierarchical porous structures; interfacial assembly; protein immobilization; protein−inorganic hybrids; supraparticles.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adsorption
  • Biomimetics*
  • Nanoparticles
  • Nanostructures*
  • Porosity
  • Proteins / chemistry*


  • Proteins