Controlling Protein Adsorption through Nanostructured Polymeric Surfaces

Abstract

The initial host response to healthcare materials' surfaces after implantation is the adsorption of proteins from blood and interstitial fluids. This adsorbed protein layer modulates the biological/cellular responses to healthcare materials. This stresses the significance of the surface protein assembly for the biocompatibility and functionality of biomaterials and necessitates a profound fundamental understanding of the capability to control protein–surface interactions. This review, therefore, addresses this by systematically analyzing and discussing strategies to control protein adsorption on polymeric healthcare materials through the introduction of specific surface nanostructures. Relevant proteins, healthcare materials' surface properties, clinical applications of polymer healthcare materials, fabrication methods for nanostructured polymer surfaces, amorphous, semicrystalline and block copolymers are considered with a special emphasis on the topographical control of protein adsorption. The review shows that nanostructured polymer surfaces are powerful tools to control the amount, orientation, and order of adsorbed protein layers. It also shows that the understanding of the biological responses to such ordered protein adsorption is still in its infancy, yet it has immense potential for future healthcare materials. The review, which is—as far as it is known—the first one discussing protein adsorption on nanostructured polymer surfaces, concludes with highlighting important current research questions.

Protein adsorption on biomaterials' surfaces is a very complex process impacting biocompatibility of healthcare materials. Nanostructured surfaces are recognized as a powerful tool to control protein–surface interactions. This review highlights recent studies relating nanostructured polymer surfaces represented by synthetic amorphous homopolymers, semicrystalline polymers, and block copolymers, and their ability to control the amount, conformation, and selectivity of protein adsorption.

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