Abstract
PEGylation of proteins remains an integral part of macromolecular therapeutics due to its well-known benign effects and pharmacokinetic enhancement properties. We report herein that PEGylation can be taken to the next level of complexity and dynamic behaviour by introducing highly stable but responsive supramolecular handles. By attaching small boronic acid groups onto proteins and salicylhydroxamate moiety to end-functionalise PEG chains, we demonstrate a comprehensive study on the facile assembly/disassembly of a core-shell protein–polymer architecture using fluorescence and microscale thermophoresis on a macromolecular level. In addition, we demonstrate that both the activity and cellular transfer of functional proteins remained conserved throughout the assembly process thus establishing a rapid and orthogonal strategy towards protein PEGylation.
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