title: Design of a reversible inversed pH-responsive caged protein.
abstract: Controlling the self-assembly behavior of caged proteins expands their potential applications in nanotechnology. While the structure of a caged E2 protein from pyruvate dehydrogenase is inert to any pH change, the incorporation of switchable GALA peptide that undergoes a coil-to-helix transition at acidic pH modulates its self-assembly property. By substituting the native α-helix at the C-terminus of the E2 protein with the GALA peptide, we report the first engineered caged protein with reversible inversed pH-responsive behavior. The redesigned caged E2 protein assumes an assembly profile that is distinct from the native state; it disassembles at pH 7.0 and self-assembles at pH 4.0 in a reversible manner. This unique reversible pH trigger suggests the applicability of the self-assembly control on other multi-subunit macromolecules.
authors.affiliation: Division of Bioengineering, School of Chemical and Biomedical Engineering, Nanyang Technological University, Singapore 637457. SLim@ntu.edu.sg.
authors.forename: Tao
authors.initials: T
authors.lastname: Peng
authors.forename: Hwankyu
authors.initials: H
authors.lastname: Lee
authors.forename: Sierin
authors.initials: S
authors.lastname: Lim
mesh_terms: D006863:Hydrogen-Ion Concentration; D053769:Nanocapsules / Q000737:chemistry*; D049329:Nanostructures / Q000737:chemistry*; D036103:Nanotechnology; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D015202:Protein Engineering / Q000379:methods*
chemical_list: D053769:Nanocapsules; D010455:Peptides; C066951:GALA peptide