Designing two self-assembly mechanisms into one viral capsid protein
| Autor: | Joseph Che Yen Wang, Roeland J. M. Nolte, Jan C. M. van Hest, Jeroen J. L. M. Cornelissen, Chenglei Li, Mark B. van Eldijk, Adam Zlotnick, Inge J. Minten |
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| Přispěvatelé: | Biomolecular Nanotechnology, Faculty of Science and Technology, ICMS Business Operations |
| Rok vydání: | 2012 |
| Předmět: |
Models
Molecular IR-85016 Chemistry Structural protein General Chemistry Hydrogen-Ion Concentration Biochemistry Fusion protein Bio-Organic Chemistry Bromovirus Catalysis Nanocapsules Article Crystallography Colloid and Surface Chemistry Capsid METIS-293504 Biophysics Copolymer Capsid Proteins Self-assembly Peptides Physical Organic Chemistry |
| Zdroj: | Journal of the American Chemical Society, 134(45), 18506-18509. American Chemical Society Journal of the American Chemical Society, 134, 18506-18509 Journal of the American Chemical Society, 134, 45, pp. 18506-18509 |
| ISSN: | 0002-7863 |
| DOI: | 10.1021/ja308132z |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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