Abstract
Fabrication and development of nanoscale materials with tunable structural and functional properties require a dynamic arrangement of nanoparticles on architectural templates. The function of nanoparticles not only depends on the property of the nanoparticles but also on their spatial orientations. Proteins with self-assembling properties which can be genetically engineered to varying architectural designs for scaffolds can be used to develop different orientations of nanoparticles in three dimensions. Here, we report the use of naturally self-assembling bacterial micro-compartment shell protein (PduA) assemblies in 2D and its single-point mutant variant (PduA[K26A]) in 3D architectures for the reduction and fabrication of gold nanoparticles. Interestingly, the different spatial organization of gold nanoparticles resulted in a smaller size in the 3D architect scaffold. Here, we observed a two-fold increase in catalytic activity and six-fold higher affinity toward TMB (3,3′,5,5′-tetramethylbenzidine) substrate as a measure of higher peroxidase activity (nanozymatic) in the case of PduA[K26A] 3D scaffold. This approach demonstrates that the hierarchical organization of scaffold enables the fine-tuning of nanoparticle properties, thus paving the way toward the design of new nanoscale materials.
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Acknowledgements
The work is supported by Nanomission, Department of Science and Technology, India SR/NM/NB-1082/2017 to S.S. SK thanks to the Council of Scientific and Industrial Research, India for the fellowship. NKB thanks the Institute of Nanoscience and Technology, Mohali for the fellowship. The authors thank the members of the SS lab for the helpful discussion.
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Kaur, S., Bari, N.K. & Sinha, S. Varying protein architectures in 3-dimensions for scaffolding and modulating properties of catalytic gold nanoparticles. Amino Acids 54, 441–454 (2022). https://doi.org/10.1007/s00726-022-03127-7
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DOI: https://doi.org/10.1007/s00726-022-03127-7