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Author: Dedisch, Sarah × End date: 2024 × Start date: 2020 × DDC: 570 × WGL Institute: DWI ×

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    Unraveling the Mechanism and Kinetics of Binding of an LCI-eGFP-Polymer for Antifouling Coatings
    (Weinheim : Wiley-VCH, 2021) Söder, Dominik; Garay-Sarmiento, Manuela; Rahimi, Khosrow; Obstals, Fabian; Dedisch, Sarah; Haraszti, Tamás; Davari, Mehdi D.; Jakob, Felix; Heß, Christoph; Schwaneberg, Ulrich; Rodriguez-Emmenegger, Cesar
    The ability of proteins to adsorb irreversibly onto surfaces opens new possibilities to functionalize biological interfaces. Herein, the mechanism and kinetics of adsorption of protein-polymer macromolecules with the ability to equip surfaces with antifouling properties are investigated. These macromolecules consist of the liquid chromatography peak I peptide from which antifouling polymer brushes are grafted using single electron transfer-living radical polymerization. Surface plasmon resonance spectroscopy reveals an adsorption mechanism that follows a Langmuir-type of binding with a strong binding affinity to gold. X-ray reflectivity supports this by proving that the binding occurs exclusively by the peptide. However, the lateral organization at the surface is directed by the cylindrical eGFP. The antifouling functionality of the unimolecular coatings is confirmed by contact with blood plasma. All coatings reduce the fouling from blood plasma by 8894% with only minor effect of the degree of polymerization for the studied range (DP between 101 and 932). The excellent antifouling properties, combined with the ease of polymerization and the straightforward coating procedure make this a very promising antifouling concept for a multiplicity of applications.
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    Matter-tag: A universal immobilization platform for enzymes on polymers, metals, and silicon-based materials
    (New York, NY : Wiley, 2020) Dedisch, Sarah; Wiens, Annika; Davari, Mehdi D.; Söder, Dominik; Rodriguez-Emmenegger, Cesar; Jakob, Felix; Schwaneberg, Ulrich
    Enzyme immobilization is extensively studied to improve enzyme properties in catalysis and analytical applications. Here, we introduce a simple and versatile enzyme immobilization platform based on adhesion-promoting peptides, namely Matter-tags. Matter-tags immobilize enzymes in an oriented way as a dense monolayer. The immobilization platform was established with three adhesion-promoting peptides; Cecropin A (CecA), liquid chromatography peak I (LCI), and Tachystatin A2 (TA2), that were genetically fused to enhanced green fluorescent protein and to two industrially important enzymes: a phytase (from Yersinia mollaretii) and a cellulase (CelA2 from a metagenomic library). Here, we report a universal and simple Matter-tag–based immobilization platform for enzymes on various materials including polymers (polystyrene, polypropylene, and polyethylene terephthalate), metals (stainless steel and gold), and silicon-based materials (silicon wafer). The Matter-tag–based enzyme immobilization is performed at ambient temperature within minutes (<10 min) in an aqueous solution harboring the phytase or cellulase by immersing the targeted material. The peptide LCI was identified as universal adhesion promoter; LCI immobilized both enzymes on all investigated materials. The attachment of phytase-LCI onto gold was characterized with surface plasmon resonance spectroscopy obtaining a dissociation constant value (KD) of 2.9·10−8 M and a maximal surface coverage of 504 ng/cm². © 2019 The Authors. Biotechnology and Bioengineering published by Wiley Periodicals, Inc.