Nature endows life with a wide variety of sophisticated, synergistic, and highly functional protein assemblies. Following Nature's inspiration to assemble protein building blocks into exquisite nanostructures is emerging as a fascinating research field. Dictating protein assembly to obtain highly ordered nanostructures and sophisticated functions not only provides a powerful tool to understand the natural protein assembly process but also offers access to advanced biomaterials. Over the past couple of decades, the field of protein assembly has undergone unexpected and rapid developments, and various innovative strategies have been proposed. This Review outlines recent advances in the field of protein assembly and summarizes several strategies, including biotechnological strategies, chemical strategies, and combinations of these approaches, for manipulating proteins to self-assemble into desired nanostructures. The emergent applications of protein assemblies as versatile platforms to design a wide variety of attractive functional materials with improved performances have also been discussed. The goal of this Review is to highlight the importance of this highly interdisciplinary field and to promote its growth in a diverse variety of research fields ranging from nanoscience and material science to synthetic biology.

No abstract

No abstract

Stable protein one (SP1) has been demonstrated as an appealing building block to design highly ordered architectures, despite the hybrid assembly with other nano-objects still being a challenge. Herein, we developed a strategy to construct high-ordered protein nanostructures by electrostatic self-assembly of cricoid protein nanorings and globular quantum dots (QDs). Using multielectrostatic interactions between 12mer protein nanoring SP1 and oppositely charged CdTe QDs, highly ordered nanowires with sandwich structure were achieved by hybridized self-assembly. QDs with different sizes (QD1, 3-4 nm; QD2, 5-6 nm; QD3, ∼10 nm) would induce the self-assembly protein rings into various nanowires, subsequent bundles, and irregular networks in aqueous solution. Atomic force microscopy, transmission electron microscopy, and dynamic light scattering characterizations confirmed that the size of QDs and the structural topology of the nanoring play critical functions in the formation of the superstructures. Furthermore, an ordered arrangement of QDs provides an ideal scaffold for designing the light-harvesting antenna. Most importantly, when different sized QDs (e.g., QD1 and QD3) self-assembled with SP1, an extremely efficient Förster resonance energy transfer was observed on these protein nanowires. The self-assembled protein nanostructures were demonstrated as a promising scaffold for the development of an artificial light-harvesting system.

Construction of catalytic centers on natural protein aggregates is a challenging topic in biomaterial and biomedicine research. Here we report a novel construction of artificial nanoenzyme with glutathione peroxidase (GPx)-like function. By engineering the surface of tobacco mosaic virus (TMV) coat protein, the main catalytic components of GPx were fabricated on TMV protein monomers. Through direct self-assembly of the functionalized viral coat proteins, the multi-GPx centers were installed on these well-defined nanodisks or nanotubes. With the help of muti-selenoenzyme centers, the resulting organized nanoenzyme exhibited remarkable GPx activity, even approaching the level of natural GPx. The antioxidation study on subcell mitochondrial level demonstrated that virus-based nanoenzyme exerted excellent capacity for protecting cell from oxidative damage. This strategy represents a new way to develop artificial nanoenzymes.