Protecting Encapsulin Nanoparticles with Cysteine-Knot Miniproteins

Robin Klem, Mark V. De Ruiter, Jeroen J.L.M. Cornelissen* (Corresponding Author)

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

4 Citations (Scopus)
42 Downloads (Pure)

Abstract

A big hurdle for the use of protein-based drugs is that they are easily degraded by proteases in the human body. In an attempt to solve this problem, we show the possibility to functionalize TM encapsulin nanoparticles with an mEETI-II knottin miniprotein from the cysteine-stabilized knot class. The resulting particles did not show aggregation and retained part of their protease inhibitive function. This imposes a protection toward protease, in this case, trypsin, degradation of the protein cage. The used chemistry is easy to apply and thus suitable to protect other protein systems from degradation. In addition, this proof of principle opens up the use of other knottins or cysteine-stabilized knots, which can be attached to protein cages to create a heterofunctionalized protein nanocage. This allows specific targeting and tumor suppression among other types of functionalization. Overall, this is a promising strategy to protect a protein of interest which brings oral administration of protein-based drugs one step closer.

Original languageEnglish
Pages (from-to)2991-2996
Number of pages6
JournalMolecular pharmaceutics
Volume15
Issue number8
DOIs
Publication statusPublished - 6 Aug 2018

Keywords

  • UT-Hybrid-D
  • bacterial nanocompartment
  • nanocage
  • protease inhibitor
  • antibody substitute

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