Designing two self-assembly mechanisms into one viral capsid protein

M.B. van Eldijk, Joseph C. Y. Wang, I.J. Minten, Chenglei Li, A. Zlotnick, R.J.M. Nolte, J.J.L.M. Cornelissen, J.C.M. Hest, van

Research output: Contribution to journalArticleAcademicpeer-review

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

Fingerprint

Dive into the research topics of 'Designing two self-assembly mechanisms into one viral capsid protein'. Together they form a unique fingerprint.

Cite this