Abstract
In this paper, a strategy for structured monitoring of surface modifications to control protein adsorption to membrane structures is presented. The already established on-surface enzymatic digestion (oSED) method combined with nano-liquid chromatography and tandem mass spectrometry (LC-MS/MS) analysis was employed for the analysis of proteins in ventricular cerebrospinal fluid (vCSF) from neurointensive care patients. Protein adsorption was studied by in-situ sampling in a temporally resolved manner on both immobilized native and Pluronic-deactivated membranes. Deactivation was significantly reducing the protein adsorption but it also induced novel selective properties of the surface. The proposed versatile strategy will facilitate protein-biomaterial, protein-polymer, protein-protein interaction studies in the future.
Highlights
Foreign material in contact with biological matrices—such as tissue, blood, plasma or cerebrospinal fluid (CSF)—instantly attracts dissolved proteins [1,2]
When the Pluronic is dissolved in water at a concentration lower than the critical micelle concentration, the hydrophobic units interact with hydrophobic foreign material, resulting in the hydrophilic units of Pluronic protruding into the aqueous solution and forming a cilia-resembling layer
This paper describes an unbiased comparison of surface deactivated microdialysis membranes and native membranes with respect to protein adsorption
Summary
Foreign material in contact with biological matrices—such as tissue, blood, plasma or cerebrospinal fluid (CSF)—instantly attracts dissolved proteins [1,2]. When the Pluronic is dissolved in water at a concentration lower than the critical micelle concentration, the hydrophobic units interact with hydrophobic foreign material, resulting in the hydrophilic units of Pluronic protruding into the aqueous solution and forming a cilia-resembling layer. This layer impedes proteins to reach the surface due to steric hindrance and thereby the hydration of the surface is maintained. Our group compared protein adsorption to Poloxamer 407 surface modified microdialysis membranes with adsorption to unmodified membranes [6]. Poloxamer 407 is a triblock copolymer referred to Separations 2018, 5, 27; doi:10.3390/separations5020027 www.mdpi.com/journal/separations
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