Interaction and enrichment of protein on cationic polysaccharide surfaces

In this study, the interaction of fluorescein isothiocyanate functionalized bovine serum albumin (FITC-BSA) with cellulose surfaces decorated with trimethyl chitosan (TMC) is investigated. Two types of TMC, one exhibiting a lower and one with a higher degree of cationization are used for protein ads...

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Veröffentlicht in:Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2014-11, Vol.123, p.533-541
Hauptverfasser: Mohan, Tamilselvan, Findenig, Gerald, Höllbacher, Stefan, Cerny, Christoph, Ristić, Tijana, Kargl, Rupert, Spirk, Stefan, Maver, Uros, Stana-Kleinschek, Karin, Ribitsch, Volker
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Sprache:eng
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Zusammenfassung:In this study, the interaction of fluorescein isothiocyanate functionalized bovine serum albumin (FITC-BSA) with cellulose surfaces decorated with trimethyl chitosan (TMC) is investigated. Two types of TMC, one exhibiting a lower and one with a higher degree of cationization are used for protein adsorption. The adsorption is carried out at different pH values and concentrations of the protein solution. The amount, morphology and wettability of FITC-BSA coating on TMC/cellulose films are determined using quartz crystal microbalance with dissipation (QCM-D), atomic force microscopy, fluorescence microscopy and contact angle measurements. A lower pH and higher concentration of protein solution resulted in a greater amount of irreversibly adsorbed material owing to the reduced solubility and minimized electrostatic repulsion. A maximum adsorption of protein is observed on cellulose surfaces functionalized with TMC carrying a higher degree of cationization compared to TMC with a lower degree of cationization and pure cellulose surfaces at all applied concentrations and pH values. BSA is a commonly used model protein and is applied in this study to better understand its interaction with cationically rendered cellulose surfaces. Such knowledge is essential for creation of multifunctional polysaccharide-based biomaterials.
ISSN:0927-7765
1873-4367
DOI:10.1016/j.colsurfb.2014.09.053