Title: pH-Dependent Immobilization of Proteins on Surfaces Functionalized by Plasma-Enhanced Chemical Vapor Deposition of Poly(acrylic acid)- and Poly(ethylene oxide)-like Films
Citation: LANGMUIR vol. 24 no. 14 p. 7251-7261
Publication Year: 2008
JRC N°: JRC46825
ISSN: 0743-7463
URI: http://publications.jrc.ec.europa.eu/repository/handle/JRC46825
DOI: 10.1021/la8003454
Type: Articles in periodicals and books
Abstract: The interaction of the proteins bovine serum albumin (BSA), lysozyme (Lys), lactoferrin (Lf), and fibronectin (Fn) with surfaces of protein-resistant poly(ethylene oxide) (PEO) and protein-adsorbing poly(acrylic acid) (PAA) fabricated by plasma-enhanced chemical vapor deposition has been studied with quartz crystal microbalance with dissipation monitoring (QCM-D). We focus on several parameters which are crucial for protein adsorption, i.e., the isoelectric point (pI) of the proteins, the pH of the solution, and the charge density of the sorbent surfaces, with the -potential as a measure for the latter. The measurements reveal adsorption stages characterized by different segments in the plots of the dissipation vs frequency change. PEO remains protein-repellent for BSA, Lys, and Lf at pH 4-8.5, while weak adsorption of Fn was observed. On PAA, different stages of protein adsorption processes could be distinguished under most experimental conditions. BSA, Lys, Lf, and Fn generally exhibit a rapid initial adsorption phase on PAA, often followed by slower processes. The evaluation of the adsorption kinetics also reveals different adsorption stages, whereas the number of these stages does not always correspond to the structurally different phases as revealed by the D-f plots. The results presented here, together with information obtained in previous studies by other groups on the properties of these proteins and their interaction with surfaces, allow us to develop an adsorption scenario for each of these proteins, which takes into account electrostatic protein-surface and protein-protein interaction, but also the pH-dependent properties of the proteins, such as shape and exposure of specific domains.
JRC Directorate:Institute for Health and Consumer Protection Historical Collection

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