Combining Polymers with the Functionality of Proteins: New Concepts for Atom Transfer Radical Polymerization, Nanoreactors and Damage Self-reporting Materials
Nico Bruns,
Samuel Lörcher,
Katarzyna Makyła,
Jonas Pollarda,
Kasper Renggli,
Mariana Spulber
Affiliations
Nico Bruns
Adolphe Merkle Institute, University of Fribourg, Route de l'ancienne Papeterie CP 209, CH-1723 Marly 1, Switzerland; Department of Chemistry, University of Basel, Klingelbergstrasse 80, CH-4056 Basel, Switzerland. [email protected]
Samuel Lörcher
Department of Chemistry, University of Basel, Klingelbergstrasse 80, CH-4056 Basel, Switzerland
Katarzyna Makyła
Department of Chemistry, University of Basel, Klingelbergstrasse 80, CH-4056 Basel, Switzerland
Jonas Pollarda
Adolphe Merkle Institute, University of Fribourg, Route de l'ancienne Papeterie CP 209, CH-1723 Marly 1, Switzerland
Kasper Renggli
Department of Chemistry, University of Basel, Klingelbergstrasse 80, CH-4056 Basel, Switzerland
Mariana Spulber
Department of Chemistry, University of Basel, Klingelbergstrasse 80, CH-4056 Basel, Switzerland
Proteins are macromolecules with a great diversity of functions. By combining these biomolecules with polymers, exciting opportunities for new concepts in polymer sciences arise. This highlight exemplifies the aforementioned with current research results of our group. We review our discovery that the proteins horseradish peroxidase and hemoglobin possess ATRPase activity, i.e. they catalyze atom transfer radical polymerizations. Moreover, a permeabilization method for polymersomes is presented, where the photo-reaction of an ?-hydroxyalkylphenone with block copolymer vesicles yields enzyme-containing nanoreactors. A further intriguing possibility to obtain functional nanoreactors is to enclose a polymerization catalyst into the thermosome, a protein cage from the family of chaperonins. Last but not least, fluorescent proteins are discussed as mechanoresponsive molecular sensors that report microdamages within fiber-reinforced composite materials.
