Complete shift of ferritin oligomerization toward nanocage assembly via engineered protein-protein interactions

Chem Commun (Camb). 2013 May 4;49(34):3528-30. doi: 10.1039/c3cc40886h.

Abstract

Computational redesign of a dimorphic protein nano-cage at the C3-symmetrical interfaces forces it to assemble into the monomorphic cage. These monodisperse assemblies are at least 20 °C more stable than the parent. This approach adds to the toolkit of bottom-up molecular design with applications in protein engineering and hybrid nano-materials.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Cytochrome b Group / chemistry*
  • Cytochrome b Group / genetics
  • Ferritins / chemistry*
  • Ferritins / genetics
  • Mutation
  • Nanostructures / chemistry*
  • Protein Conformation
  • Protein Engineering

Substances

  • Bacterial Proteins
  • Cytochrome b Group
  • Ferritins
  • bacterioferritin