Biotransformation on Polymer–Peptide Conjugates: A Versatile Tool to Trigger Microstructure Formation†
Hans Kühnle
Max Planck Institute of Colloids and Interfaces, Research Campus Golm, 14424 Potsdam (Germany), Fax: (+49) 331-567-9502 http://www.mpikg.mpg.de/kc/boerner/
Search for more papers by this authorHans G. Börner Dr.
Max Planck Institute of Colloids and Interfaces, Research Campus Golm, 14424 Potsdam (Germany), Fax: (+49) 331-567-9502 http://www.mpikg.mpg.de/kc/boerner/
Search for more papers by this authorHans Kühnle
Max Planck Institute of Colloids and Interfaces, Research Campus Golm, 14424 Potsdam (Germany), Fax: (+49) 331-567-9502 http://www.mpikg.mpg.de/kc/boerner/
Search for more papers by this authorHans G. Börner Dr.
Max Planck Institute of Colloids and Interfaces, Research Campus Golm, 14424 Potsdam (Germany), Fax: (+49) 331-567-9502 http://www.mpikg.mpg.de/kc/boerner/
Search for more papers by this authorThe work was supported by the Deutsche Forschungsgemeinschaft (Emmy Noether BO1762/2-3) and Max Planck Society. We thank M. Antonietti, A. Thomas, E. Krause, D. Gebauer, H. Stephanowitz, A. Heilig, R. Pitschke and A. E. F. Wächtler, M. Kühnle, and Erich C.
Graphical Abstract
At the flick of a switch: Introducing phosphate moieties into (Thr-Val)X peptide aggregation domains disturbs the formation of secondary structures. This suppression is used to regulate the self-assembly of polymer–peptide conjugates. A phosphatase enzyme which hydrolyzes the phosphate esters then triggers the self-assembly process generating fibrillar aggregates (see scheme).
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