Designing two self-assembly mechanisms into one viral capsid protein.
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ABSTRACT:
SUBMITTER: van Eldijk MB
PROVIDER: S-EPMC3510441 | biostudies-literature | 2012 Nov
REPOSITORIES: biostudies-literature
Publications
Designing two self-assembly mechanisms into one viral capsid protein.
van Eldijk Mark B MB Wang Joseph C-Y JC Minten Inge J IJ Li Chenglei C Zlotnick Adam A Nolte Roeland J M RJ Cornelissen Jeroen J L M JJ van Hest Jan C M JC
Journal of the American Chemical Society 20121101 45
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 prope ...[more]
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