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- W2800694736 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." @default.
- W2800694736 created "2018-05-17" @default.
- W2800694736 creator A5006131224 @default.
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- W2800694736 date "2018-04-16" @default.
- W2800694736 modified "2023-10-10" @default.
- W2800694736 title "Modular assembly of proteins on nanoparticles" @default.
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- W2800694736 doi "https://doi.org/10.1038/s41467-018-03931-4" @default.
- W2800694736 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5902510" @default.
- W2800694736 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29662234" @default.
- W2800694736 hasPublicationYear "2018" @default.
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