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American Chemical Society, Journal of the American Chemical Society, 45(134), p. 18506-18509, 2012

DOI: 10.1021/ja308132z

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Designing Two Self-Assembly Mechanisms into One Viral Capsid Protein

Journal article published in 2012 by M. B. Eldijk, Mark B. van Eldijk, Joseph C.-Y. Wang, Inge J. Minten, Chenglei L. Li, Adam Zlotnick ORCID, Roeland J. M. Nolte ORCID, Jeroen J. L. M. Cornelissen, Jan C. M. van Hest, J. C. M. van Hest
This paper is available in a repository.
This paper is available in a repository.

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Abstract

A structural fusion protein of the thermally-responsive elastin-like polypeptide and a viral capsid protein (ELP-CP) was designed and the 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 to create a self-assembly system with new properties by combining two structural protein elements.