Precise Self-Assembly of Nanoparticles into Ordered Nanoarchitectures Directed by Tobacco Mosaic Virus Coat Protein.
Self-assembly guided by biological molecules is a promising approach for fabricating predesigned nanostructures. Protein is one such biomolecule possessing deterministic 3D crystal structure and peptide information, which acts as a good candidate for templating functional nanoparticles (fNPs). However, inadequate coordination efficacy during the establishment of interfacial interactions with fNPs makes it highly challenging to precisely fabricate designed nanostructures and functional materials. Here, a facile and robust strategy is reported for the hierarchical assembly of fNPs into ordered architectures, with unprecedentedly large sizes up to tens of micrometers, using a hollow cylinder-shaped tobacco mosaic virus coat protein (TMV disk). The rational design of the site-specific functional groups on the TMV disk not only demonstrates the powerful capability of directing various discrete fNP assemblies with high controllability but also assists in precise assembly of a TMV monolayer sheet structure for further organizing homogeneous and heterogeneous fNP periodic lattices by varying the types of fNPs. The high precision and adjustability of the pattern fashions of different fNPs unambiguously corroborate the validity of this innovative strategy, which provides a convenient route to design and assemble protein-based hierarchical ordered architectures for use in nanophotonics and nanodevices.
['Zhang|Jianting|J|', 'Zhou|Kun|K|', 'Zhang|Yejun|Y|', 'Du|Mingming|M|', 'Wang|Qiangbin|Q|https://orcid.org/0000-0001-6589-6328']
D000596:Amino Acids D001665:Binding Sites D036022:Capsid Proteins D053758:Nanoparticles D049329:Nanostructures D010316:Particle Size D011485:Protein Binding D014027:Tobacco Mosaic Virus D014764:Viral Proteins
self-assembly tobacco mosaic virus interfacial interactions nanoparticle lattices protein structures