Construction of a Ball‐and‐Spike Protein Supramolecule

Abstract

On the ball: Fusion of gp5C (spike) to LisDps (ball) through a flexible linker connecting the respective C and N termini allowed the engineered construction of a ball‐and‐spike protein supramolecule. The two symmetric protein components self‐assemble to form a large protein supramolecule made of artificial components.

Molecular Design of Heteroprotein Assemblies Providing a Bionanocup as a Chemical Reactor

“…Bioarchitectures containing synthetic molecules are very attractive candidates for the construction of catalysts, sensors, and materials with novel properties 1–11. Protein self‐assemblies are especially suitable for these purposes because they can lead to various different nanoscale cage architectures.…”

Ferritin as a bionano-particulate emulsifier

“…The inner and outer diameters of the protein shell are approximately 7 nm and 12 nm, respectively, and there are atomically small channels along three fold axis through which ions can center the cavity [21]. Ferritin has been extensively used in a variety of applications, such as reaction vessel for synthesizing various metal nanoparticles [22], self-assembling tool for fabricating two dimensional array of metal nanoparticles applying for floating nanodot gate memory devices [23], nanoblock for constructing supramolecular structure [24] and carriers for drug delivery [25].…”

Higher Order Assembly of Virus‐like Particles (VLPs) Mediated by Multi‐valent Protein Linkers

“…The fusion of the Dec to the N‐terminus of Li Dps subunit did not disrupt the self‐assembly of the spherical cage‐like structure of Li Dps, and hence it is likely that four of Dec trimers are displayed on the surface of Li Dps, projecting the N‐terminus of Dec towards the outside of the cage (Figure c). This structure was anticipated based on similar protein engineering strategies that have been successfully explored to design Li Dps fused with the β‐helix domains of gp5 from bacteriophage T4 and the ferritin protein cage fused with the hemagglutinin protein of influenza virus where a symmetry match between the cage and the fusion protein ensures the proper quaternary structure of the construct. For example, in the case of the paper reported by Sugimoto et al , the C‐terminus of β‐helix domains of gp5 from bacteriophage T4, which is a trimeric rod‐shape protein with three‐fold symmetry, is fused with the N‐terminus of LiDps, and the fusion protein is reported to be assembled to a cage‐like structure with four spikes due to the gp5 domain …”

“…Mutagenesis and Purification of Dec‐Dps Fusion Protein : The C‐terminus of wt Dec was fused to the N‐terminus of wild type Dps protein derived from Listeria innocua ( Li Dps) that was inspired by previous studies . The N‐terminus of Li Dps is exposed to exterior surface of the cage .…”