%0 Journal Article
%T A Strep-tag Imprinted Polymer Platform for Heterogenous Bio(electro)catalysis.
%A Yarman A
%A Waffo AFT
%A Katz S
%A Bernitzky CCM
%A Kovács N
%A Borrero P
%A Frielingsdorf S
%A Supala E
%A Dragelj J
%A Kurbanoglu S
%A Neumann B
%A Lenz O
%A Gyurcsányi RE
%A Mroginski MA
%A Wollenberger U
%A Scheller FW
%A Caserta G
%A Zebger I
%J Angew Chem Int Ed Engl
%V 0
%N 0
%D 2024 Jul 9
%M 38979660
%F 16.823
%R 10.1002/anie.202408979
%X Molecularly imprinted polymers (MIPs) are artificial receptors equipped with selective recognition sites for target molecules. One of the most promising-strategies for protein MIPs relies on the exploitation of short surface-exposed protein fragments, termed epitopes, as templates to imprint binding sites in a polymer scaffold for a desired protein. However, the lack of high-resolution structural data of flexible surface-exposed regions challenges the selection of suitable epitopes. Here, we addressed this drawback by developing a polyscopoletin-based MIP that recognizes recombinant proteins via the widely used Strep-tag II affinity peptide. Electrochemistry, surface-sensitive spectroscopy, and molecular dynamics simulations were employed to ensure an utmost control of the Strep-MIP electrosynthesis. The functionality of this novel platform was verified with two Strep-tag labeled enzymes: an O2-tolerant [NiFe]-hydrogenase, and an alkaline phosphatase. The enzymes preserved their biocatalytic activities after multiple utilization confirming the efficiency of Strep-MIP as a general biocompatible platform to confine recombinant proteins for exploitation in biotechnology.