Modular assembly of proteins on nanoparticles. / Ma, Wenwei; Saccardo, Angela ; Roccatano, Danilo ; Aboagye-Mensah, Dorothy ; Alkaseem, Mohammad; Jewkes, Matthew ; Di Nezza, Francesca ; Baron, Mark ; Soloviev, Mikhail; Ferrari, Enrico.

In: Nature Communications, Vol. 9, 1489, 16.04.2018, p. 1-9.

Research output: Contribution to journalArticlepeer-review

  • Wenwei Ma
  • Angela Saccardo
  • Danilo Roccatano
  • Dorothy Aboagye-Mensah
  • Mohammad Alkaseem
  • Matthew Jewkes
  • Francesca Di Nezza
  • Mark Baron
  • Mikhail Soloviev
  • Enrico Ferrari


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
Publication statusPublished - 16 Apr 2018
This open access research output is licenced under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported License.

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