Programming Self-Assembly of Tobacco Mosaic Virus Coat Proteins at Pickering Emulsion Interfaces for Nanorod-Constructed Capsules

Pickering emulsion constructions on nanorods with high aspect ratio are a great challenge because of the geometry restrictions. On the basis of the theory that the stability of Pickering emulsion is highly dependent on the size and amphiphilicity of the nanoparticle at fluid interfaces, we report a novel strategy to fabricate long-time stable Pickering emulsion consisting of tobacco mosaic virus (TMV)-like nanorods through the programming self-assembly of TMV coat protein (TMVCP). The first step is the self-assembly of amphiphilic TMVCP at Pickering emulsion interfaces, and the second step is the in situ interfacial self-assembly of TMVCP into nanorods with increased particle size. The robust capsules can be further fabricated through cross-linking of the proteins. By taking advantage of both the amphiphilicity of TMVCP and the subsequent size growth induced by TMVCP self-assembly, this work provides a powerful strategy for constructing robust capsules consisting of nanorods with high aspect ratio, which may show potential applications for drug delivery and virus recognition.