Nanohedra: Using symmetry to design self assembling protein cages, layers, crystals, and filaments

Abstract

A general strategy is described for designing proteins that self assemble into large symmetrical nanomaterials, including molecular cages, filaments, layers, and porous materials. In this strategy, one molecule of protein A, which naturally forms a self-assembling oligomer, A n, is fused rigidly to one molecule of protein B, which forms another self-assembling oligomer, B m. The result is a fusion protein, A-B, which self assembles with other identical copies of itself into a designed nanohedral particle or material, (A-B) p. The strategy is demonstrated through the design, production, and characterization of two fusion proteins: a 49-kDa protein designed to assemble into a cage approximately 15 nm across, and a 44-kDa protein designed to assemble into long filaments approximately 4 nm wide. The strategy opens a way to create a wide variety of potentially useful protein-based materials, some of which share similar features with natural biological assemblies.

Hierarchical Self‐Assembly of One‐Dimensional Streptavidin Bundles as a Collagen Mimetic for the Biomineralization of Calcite

“…Typical examples include protein fibrils, [7,8] ferritin, [9,10] S-layers, [11][12][13] antibodies, [14] peptide amphiphiles, [15] capsids, [16][17][18][19] leucine zippers, [20] etc. [21][22][23][24][25][26] Controlled protein aggregation is a critical process in many areas, ranging from biomineralization [27] to neurodegenerative diseases. [28] In contrast with molecular tectonics, however, [5,29] the de novo design of higher-order architectures by using proteins as building blocks (e.g.…”

“…protein tectonics) remains challenging. [21][22][23][24][30][31][32][33][34] In the spirit of coordination polymers, we reasoned that one may exploit the versatility of transition-metal connectors in conjunction with proteins bearing tethered ligands to create discrete one-, two-, or three-dimensional metalorganic protein frameworks (MOPF; Figure 1). For this proof-of-principle study, we used a linear Fe(terpy) 2 moiety (terpy = terpyridine) bearing four biotin anchors, [Fe(Biot 2 -terpy) 2 ] 2+ complex (the connector), in conjunction with streptavidin (hereafter referred to as Sav, the linker) to afford a one-dimensional MOPF.…”

Hyperthin nanochains composed of self-polymerizing protein shackles

“…A protein with a pair of binding partners on opposite sides would polymerize controllably in a manner depending on the nature of the binding partners. This strategy has been used previously [16][17][18][19][20][21][22][23] , but there remained several problems: for example, chemical modifications of monomers to make binding sites are often necessary [16][17][18][19][20] , single strands of the polymers are supposed to break easily and to be not stable for long periods in dilute solution because they are held together by noncovalent interactions 16,17,[21][22][23] , and single strands of the polymers often assemble in an uncontrolled manner 21,22 .…”

Supramolecular Wireframe DNA Polyhedra: Assembly and Applications

“…It is notable that 3D wireframe polyhedra based on RNA [89][90][91][92][93][94] and protein [95][96][97][98][99] have also appeared in recent literatures. In the case of in vivo applications, some fundamental issues need to be addressed for the polyhedral DNA structures: (1) how to build a more robust DNA polyhedron with increased in vivo circulation time; (2) how to target a specific tumor cell and a subcellular region with a DNA polyhedron, and (3) how to improve cellular uptake efficiency and facilitate lysosomal escape.…”