Structure of a designed protein cage that self-assembles into a highly porous cube. Academic Article uri icon

abstract

  • Natural proteins can be versatile building blocks for multimeric, self-assembling structures. Yet, creating protein-based assemblies with specific geometries and chemical properties remains challenging. Highly porous materials represent particularly interesting targets for designed assembly. Here, we utilize a strategy of fusing two natural protein oligomers using a continuous alpha-helical linker to design a novel protein that self assembles into a 750kDa, 225 diameter, cube-shaped cage with large openings into a 130 diameter inner cavity. A crystal structure of the cage showed atomic-level agreement with the designed model, while electron microscopy, native mass spectrometry and small angle X-ray scattering revealed alternative assembly forms in solution. These studies show that accurate design of large porous assemblies with specific shapes is feasible, while further specificity improvements will probably require limiting flexibility to select against alternative forms. These results provide a foundation for the design of advanced materials with applications in bionanotechnology, nanomedicine and material sciences.

published proceedings

  • Nat Chem

altmetric score

  • 172.534

author list (cited authors)

  • Lai, Y., Reading, E., Hura, G. L., Tsai, K., Laganowsky, A., Asturias, F. J., ... Yeates, T. O.

citation count

  • 234

complete list of authors

  • Lai, Yen-Ting||Reading, Eamonn||Hura, Greg L||Tsai, Kuang-Lei||Laganowsky, Arthur||Asturias, Francisco J||Tainer, John A||Robinson, Carol V||Yeates, Todd O

publication date

  • January 2014