Designing two self-assembly mechanisms into one viral capsid protein

M.B. van Eldijk, J.C.Y. Wang, I.J. Minten, C.L. Li, A. Zlotnick, R.J.M. Nolte, Jeroen Johannes Lambertus Maria Cornelissen, J.C.M. van Hest

Research output: Contribution to journalArticleAcademicpeer-review

76 Citations (Scopus)

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 languageUndefined
Pages (from-to)18506-18509
Number of pages3
JournalJournal of the American Chemical Society
Volume134
Issue number45
DOIs
Publication statusPublished - 2012

Keywords

  • METIS-293504
  • IR-85016

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