Modular assembly of proteins on nanoparticles

Wenwei Ma, Angela Saccardo, Danilo Roccatano, Dorothy Aboagye-Mensah, Mohammad Alkaseem, Matthew Jewkes, Francesca Di Nezza, Mark Baron, Mikhail Soloviev and Enrico Ferrari ()
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Wenwei Ma: University of Lincoln
Angela Saccardo: University of Lincoln
Danilo Roccatano: University of Lincoln
Dorothy Aboagye-Mensah: University of Lincoln
Mohammad Alkaseem: University of Lincoln
Matthew Jewkes: University of Lincoln
Francesca Di Nezza: University of Molise
Mark Baron: University of Lincoln
Mikhail Soloviev: Royal Holloway University of London
Enrico Ferrari: University of Lincoln

Nature Communications, 2018, vol. 9, issue 1, 1-9

Abstract: Abstract 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.

Date: 2018
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DOI: 10.1038/s41467-018-03931-4

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