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

93 Scopus citations


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
Issue number45
StatePublished - Nov 14 2012

All Science Journal Classification (ASJC) codes

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


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