In this contribution we present the creation of matrices for controlled protein deposition whereas cellulose ultrathin films are equipped with BSA (Bovine Serum Albumin) via cationization of the surface by tailor made cationic celluloses. The extent of protein affinity to these surfaces is controlled by the solubility and charge density of the cationic cellulose derivative. This effect is investigated at the example of fluorescently labeled BSA at different concentrations and pH values. The total amount of deposited protein on the surfaces is quantified by means of QCM-D (Quartz Crystal Microbalance with Dissipation Monitoring, wet mass) and MP-SPR (Multi-Parameter Surface Plasmon Resonance, dry mass). Furthermore the amount of coupled water is obtained by combination of QCM-D and MP-SPR data. It can be shown that the tuning of protein adsorption is realizable over a wide range (0.6-3.9 mg dry mass m<sup>-2</sup>) by varying the type of used cationic cellulose derivative and the applied adsorption conditions. Additionally, patterned cellulose thin films have been prepared and cationic celluloses were adsorbed in a similar fashion as in the QCM-D and MP-SPR experiments. These cationic surfaces have been loaded with fluorescently labeled BSA in different concentrations by an automatized spotting apparatus. A correlation between the amount of deposited protein and the fluorescence intensity is established.

Triggering protein adsorption on tailored cationic cellulose surfaces

249th National Meeting (2015)

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