4.8 Article

Designing Two Self-Assembly Mechanisms into One Viral Capsid Protein

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JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 134, 期 45, 页码 18506-18509

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AMER CHEMICAL SOC
DOI: 10.1021/ja308132z

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  1. Dutch Polymer Institute
  2. Chemical Council of the National Science Foundation
  3. NIH [R01 AI077688]

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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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