Self-assembled architectures from biohybrid triblock copolymers.
The synthesis and self-assembly behavior of biohybrid ABC triblock copolymers consisting of a synthetic diblock, polystyrene-b-polyethylene glycol (PSm-b-PEG113), where m is varied, and a hemeprotein, myoglobin (Mb) or horse radish peroxidase (HRP), is described. The synthetic diblock copolymer is first functionalized with the heme cofactor and subsequently reconstituted with the apoprotein or the apoenzyme to yield the protein-containing ABC triblock copolymer. The obtained amphiphilic block copolymers self-assemble in aqueous solution into a large variety of aggregate structures. Depending on the protein and the polystyrene block length, micellar rods, vesicles, toroids, figure eight structures, octopus structures, and spheres with a lamellar surface are formed.
Reynhout
Irene C
IC
Institute for Molecules and Materials, Radboud University Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands.
Cornelissen
Jeroen J L M
JJ
Nolte
Roeland J M
RJ
D006735:Horseradish Peroxidase / Q000737:chemistry*; D008823:Micelles; D015394:Molecular Structure; D009211:Myoglobin / Q000737:chemistry*; D010316:Particle Size; D011092:Polyethylene Glycols / Q000737:chemistry*; D011108:Polymers / Q000138:chemical synthesis* / Q000737:chemistry; D011137:Polystyrenes / Q000737:chemistry*; D013501:Surface-Active Agents / Q000138:chemical synthesis / Q000737:chemistry
D008823:Micelles; D009211:Myoglobin; D011108:Polymers; D011137:Polystyrenes; D013501:Surface-Active Agents; D011092:Polyethylene Glycols; D006735:Horseradish Peroxidase