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, Enrico Ferrari

Research output: Contribution to journalArticlepeer-review

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.
Original languageEnglish
Article number1489
Pages (from-to)1-9
Number of pages9
JournalNature Communications
Volume9
DOIs
Publication statusPublished - 16 Apr 2018

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