Tunable Assembly of Protein Enables Fabrication of Platinum Nanostructures with Different Catalytic Activity

Proteins are promising biofunctional units for the construction of nanomaterials (NMs) due to their abundant binding sites, intriguing self-assembly properties, and mild NM synthetic conditions. Tobacco mosaic virus coat protein (TMVCP) is a protein capable of self-assembly into distinct morphologies depending on the solution pH and ionic strength. Herein, we report the use of TMVCP as a building block to organize nanosized platinum into discrete nanorings and isolated nanoparticles by varying the solution pH to modulate the protein assembly state. Compared with a commercial Pt/C catalyst, the TMVCP-templated platinum materials exhibited significant promotion of the catalytic activity and stability toward methanol electrooxidation in both neutral and alkaline conditions. The enhanced catalytic performance is likely facilitated by the protein support. Additionally, Pt nanorings outperformed isolated nanoparticles, although they are both synthesized on TMVCP templates. This could be due to the higher mechanical stability of the protein disk structure and possible cooperative effects between adjacent nanoparticles in the ring with narrow interparticle spacing.

Automated summary

Proteins are promising biofunctional units for constructing nanomaterials due to their self-assembly properties, and can modulate the catalytic performance of nanosized platinum by varying solution pH. The mechanical stability and cooperative effects between nanoparticles in the ring structure may contribute to the enhanced catalytic activity of the protein-templated platinum materials.