Precise protein assembly of array structures

Abstract

The assembly of proteins into various nano-objects with regular and periodic microstructures, i.e. protein arrays, is a fast-growing field in materials science. Due to the structural complexity of proteins, reports in this field are still quite limited. In this review, we summarize the recent developments in protein array construction by different driving forces, including electrostatic interactions, metal-ligand interactions, molecular recognition and protein-protein interactions. In line with our particular interest, assemblies driven by molecular recognition are particularly explored. Finally, functionalities of the obtained protein arrays are briefly discussed.

Highly Ordered Self‐Assembly of Native Proteins into 1D, 2D, and 3D Structures Modulated by the Tether Length of Assembly‐Inducing Ligands

“…[1] In nature, proteins self-assemble into different structures in nano-or micrometer scale with highly ordered patterns, [2] forexample, virus capsids, [3] actin filaments, [4] microtubules, [5] and bacteria S-layers [6] .T hese attractive structures have stimulated strong motivation for programming proteins into various nanoobjects, [7] including oligomers, [8a,b] zero-dimensional (0D) nanocages, [8b,c] 1D fibers, [9] nanotubes, [10] 2D nanosheets, [11] nanorings, [12] and 3D frameworks [13] . [1] In nature, proteins self-assemble into different structures in nano-or micrometer scale with highly ordered patterns, [2] forexample, virus capsids, [3] actin filaments, [4] microtubules, [5] and bacteria S-layers [6] .T hese attractive structures have stimulated strong motivation for programming proteins into various nanoobjects, [7] including oligomers, [8a,b] zero-dimensional (0D) nanocages, [8b,c] 1D fibers, [9] nanotubes, [10] 2D nanosheets, [11] nanorings, [12] and 3D frameworks [13] .…”

“…These results introduce an easy strategy to control the assembly structure and dimension, whichcould shed light on controlled protein assembly.Proteins are remarkable building blocks for the fabrication of different functional materials because of their enormous structural complexity and intrinsic functions. [1] In nature, proteins self-assemble into different structures in nano-or micrometer scale with highly ordered patterns, [2] forexample, virus capsids, [3] actin filaments, [4] microtubules, [5] and bacteria S-layers [6] .T hese attractive structures have stimulated strong motivation for programming proteins into various nanoobjects, [7] including oligomers, [8a,b] zero-dimensional (0D) nanocages, [8b,c] 1D fibers, [9] nanotubes, [10] 2D nanosheets, [11] nanorings, [12] and 3D frameworks [13] .…”

Self-assembled nanoreactors based on peptides and proteins

“…Recently, hierarchical organization of protein assemblies into array structures has gained the interest of researchers. Electrostatic interactions, metal-ligand interactions, molecular recognition and protein-protein interactions are known to drive this hierarchical self-assembly [77] and CCMV [78], P22 [79] and ferritin [80] nanocages have been incorporated in crystalline structures and metamaterials. Combining this hierarchical organization with protein nanocage-based nanoreactors can give rise to array structures that incorporate various catalytic functions with high level of positional control.…”

Highly Ordered Self‐Assembly of Native Proteins into 1D, 2D, and 3D Structures Modulated by the Tether Length of Assembly‐Inducing Ligands

“…However, most natural proteins could be treated as colloidal particles without canonical interacting motifs for precise organization . To achieve regular protein packing structures in the laboratory, intensively engineered proteins with well‐selected geometry and symmetry are always employed to control protein–protein interactions (PPIs), which highly depend on the accuracy of the protein design .…”