biostudies-literaturevan Eldijk MBNIAID NIH HHS18506-9https://www.ebi.ac.uk/biostudies/studies/S-EPMC3510441biostudies-literatureUnknown134(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 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.Journal of the American Chemical SocietyDesigning two self-assembly mechanisms into one viral capsid protein.PMC3510441R01 AI077688van Eldijk MBvan Hest JCMinten IJLi CCornelissen JJWang JCNolte RJZlotnick AfalseDesigning two self-assembly mechanisms into one viral capsid protein.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.2012-01-01T00:00:00Z2012 Nov2024-11-09T15:05:49.43Z2019-03-27T01:01:12ZS-EPMC35104412310193710.1021/ja308132z