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Application: 1) Invited speaker
pH Responsive Janus-like Supramolecular Fusion Proteins for Functional Protein Delivery
Kaloian Koynov, Christoph Meier, and Tanja Weil*
Institute of Organic Chemistry III, Macromolecular Chemistry, University of Ulm, Albert-Einstein-Allee 11, D-89081 Ulm, Germany
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A facile, noncovalent solid-phase immobilization platform is described to assemble Janus-like supramolecular fusion proteins that are responsive to external stimuli. A chemically postmodified transporter protein, DHSA, is fused with (imino)biotinylated cargo proteins via an avidin adaptor with a high degree of spatial control. Notably, the derived heterofusion proteins are able to cross cellular membranes, dissociate at acidic pH due to the iminobiotin linker and preserve the enzymatic activity of the cargo proteins β-galactosidase and the enzymatic subunit of Clostridium botulinum C2 toxin. The mix-and-match strategy described herein opens unique opportunities to access macromolecular architectures of high structural definition and biological activity, thus complementing protein ligation and recombinant protein expression techniques.
Noncovalent solid-phase immobilization platform
Keywords: Noncovalent, Solid-phase, immobilization, DHSA, Galactosidase
References
[1] Tannock, I. F.; Rotin, D. Cancer Res. 1989, 49, 4373– 4384.
Acknowledgement: Project supported by the BMBF Project Biotechnologie 2020+, ERC Synergy Grant 319130-BioQ and the German Research Foundation.