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Nat Commun. 2018 Apr 16;9(1):1489. doi: 10.1038/s41467-018-03931-4.

Modular assembly of proteins on nanoparticles.

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College of Science, University of Lincoln, Brayford Pool, Lincoln, LN6 7TS, UK.
Department of Bioscience and Territory, University of Molise, Contrada Fonte Lappone, 86090, Pesche, Italy.
School of Biological Sciences, Royal Holloway University of London, Egham Hill, Egham, TW20 0EX, UK.
College of Science, University of Lincoln, Brayford Pool, Lincoln, LN6 7TS, UK.


Generally, the high diversity of protein properties necessitates the development of unique nanoparticle bio-conjugation methods, optimized for each different protein. Here we describe a universal bio-conjugation approach which makes use of a new recombinant fusion protein combining two distinct domains. The N-terminal part is Glutathione S-Transferase (GST) from Schistosoma japonicum, for which we identify and characterize the remarkable ability to bind gold nanoparticles (GNPs) by forming gold-sulfur bonds (Au-S). The C-terminal part of this multi-domain construct is the SpyCatcher from Streptococcus pyogenes, which provides the ability to capture recombinant proteins encoding a SpyTag. Here we show that SpyCatcher can be immobilized covalently on GNPs through GST without the loss of its full functionality. We then show that GST-SpyCatcher activated particles are able to covalently bind a SpyTag modified protein by simple mixing, through the spontaneous formation of an unusual isopeptide bond.

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