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

doi:10.1021/ja308132z

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 journal › Article › Academic › peer-review

91 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 language	Undefined
Pages (from-to)	18506-18509
Number of pages	3
Journal	Journal of the American Chemical Society
Volume	134
Issue number	45
DOIs	https://doi.org/10.1021/ja308132z
Publication status	Published - 2012

Keywords

METIS-293504
IR-85016

Access to Document

10.1021/ja308132z

Cite this

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title = "Designing two self-assembly mechanisms into one viral capsid protein",

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.",

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T1 - Designing two self-assembly mechanisms into one viral capsid protein

AU - van Eldijk, M.B.

AU - Wang, J.C.Y.

AU - Minten, I.J.

AU - Li, C.L.

AU - Zlotnick, A.

AU - Nolte, R.J.M.

AU - Cornelissen, Jeroen Johannes Lambertus Maria

AU - van Hest, J.C.M.

PY - 2012

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AB - 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.

KW - METIS-293504

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M3 - Article

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SP - 18506

EP - 18509

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

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