Unraveling the Mechanism and Kinetics of Binding of an LCI‐eGFP‐Polymer for Antifouling Coatings
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 macro...
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Published in | Macromolecular bioscience Vol. 21; no. 9; pp. e2100158 - n/a |
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Main Authors | , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Germany
Wiley Subscription Services, Inc
01.09.2021
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Subjects | |
Online Access | Get full text |
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Summary: | 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.
Protein‐polymer conjugates are designed to adhere to surfaces and confer antifouling properties. The mechanism and kinetics of binding of LCI‐eGFP‐pHPMA hybrid macromolecules are unraveled by surface plasmon resonance, X‐ray reflectivity, and atomic force microscopy. Molecular adsorption of only 168 ng cm−2 of this hybrid molecule provides coatings with repellence to blood plasma on par with polymer brushes. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1616-5187 1616-5195 |
DOI: | 10.1002/mabi.202100158 |