title: Designing two self-assembly mechanisms into one viral capsid protein.
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.
authors.affiliation: Institute for Molecules and Materials, Radboud University Nijmegen, The Netherlands.
authors.forename: Mark B
authors.initials: MB
authors.lastname: van Eldijk
authors.forename: Joseph C-Y
authors.initials: JC
authors.lastname: Wang
authors.forename: Inge J
authors.initials: IJ
authors.lastname: Minten
authors.forename: Chenglei
authors.initials: C
authors.lastname: Li
authors.forename: Adam
authors.initials: A
authors.lastname: Zlotnick
authors.forename: Roeland J M
authors.initials: RJ
authors.lastname: Nolte
authors.forename: Jeroen J L M
authors.initials: JJ
authors.lastname: Cornelissen
authors.forename: Jan C M
authors.initials: JC
authors.lastname: van Hest
mesh_terms: D017795:Bromovirus / Q000737:chemistry*; D036022:Capsid Proteins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry
chemical_list: D036022:Capsid Proteins; D010455:Peptides