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

doi:10.1021/ja308132z

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

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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 language	English
Pages (from-to)	18506-18509
Number of pages	4
Journal	Journal of the American Chemical Society
Volume	134
Issue number	45
DOIs	https://doi.org/10.1021/ja308132z
Publication status	Published - 14 Nov 2012

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AU - Nolte, R.J.M.

AU - Cornelissen, J.J.L.M.

AU - Hest, van, J.C.M.

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Designing two self-assembly mechanisms into one viral capsid protein

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