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 (US) |
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Pages (from-to) | 18506-18509 |
Number of pages | 4 |
Journal | Journal of the American Chemical Society |
Volume | 134 |
Issue number | 45 |
DOIs | |
State | Published - Nov 14 2012 |
All Science Journal Classification (ASJC) codes
- Catalysis
- General Chemistry
- Biochemistry
- Colloid and Surface Chemistry