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Designing two self-assembly mechanisms into one viral capsid protein

  • Mark B. Van Eldijk
  • , Joseph C.Y. Wang
  • , Inge J. Minten
  • , Chenglei Li
  • , Adam Zlotnick
  • , Roeland J.M. Nolte
  • , Jeroen J.L.M. Cornelissen
  • , Jan C.M. Van Hest

Research output: Contribution to journalArticlepeer-review

Abstract

ELP-CP, a structural fusion protein of the thermally responsive elastin-like polypeptide (ELP) and a viral capsid protein (CP), was designed, and its assembly properties were investigated. Interestingly, this protein-based block copolymer could be self-assembled via two mechanisms into two different, well-defined nanocapsules: (1) pH-induced assembly yielded 28 nm virus-like particles, and (2) ELP-induced assembly yielded 18 nm virus-like particles. The latter were a result of the emergent properties of the fusion protein. This work shows the feasibility of creating a self-assembly system with new properties by combining two structural protein elements.

Original languageEnglish (US)
Pages (from-to)18506-18509
Number of pages4
JournalJournal of the American Chemical Society
Volume134
Issue number45
DOIs
StatePublished - Nov 14 2012

All Science Journal Classification (ASJC) codes

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry

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