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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.

Author information

1
College of Science, University of Lincoln, Brayford Pool, Lincoln, LN6 7TS, UK.
2
Department of Bioscience and Territory, University of Molise, Contrada Fonte Lappone, 86090, Pesche, Italy.
3
School of Biological Sciences, Royal Holloway University of London, Egham Hill, Egham, TW20 0EX, UK.
4
College of Science, University of Lincoln, Brayford Pool, Lincoln, LN6 7TS, UK. eferrari@lincoln.ac.uk.

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.

PMID:
29662234
PMCID:
PMC5902510
DOI:
10.1038/s41467-018-03931-4
[Indexed for MEDLINE]
Free PMC Article

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