In this work, QCM (Quartz Crystal Microbalance) crystal surfaces were analyzed in order to study the behavior of proteins attachment on fouling substrates. In this context, covalent and non covalent immobilization of different proteins (BSA, collagen) has been investigated. For the non covalent immobilization, silicon dioxide coated QCM crystals have been used whilst the covalent immobilization has been obtained via plasma polymerized acrylic acid film (ppAA) deposited onto the QCM substrates. Two different activation processes, namely reaction with trifluoroacetic anhydride (TFAA) and 1-ethyl-3,3-dimethyl carbodiimide (EDC) and N-hydroxysuccinimide (NHS) have been studied.
After the QCM experiments, all samples have been analyzed with XPS and ToF-SIMS to gain information on the surface chemistry and composition. Results indicate that the protein adsorption process depends on protein concentration, whilst the complement activation effectiveness depends on protein type. In particular, for the BSA, XPS and QCM data show a greater immobilization in the case of EDC/NHS activation respect to the TFAA, whilst in the case of collagen, only the EDC/NHS activation was able to yield covalent coupling.
STROLA Samy;
CECCONE Giacomo;
GILLILAND Douglas;
VALSESIA Andrea;
VIEIRA LISBOA Patricia;
ROSSI Francois;
2010-07-20
JOHN WILEY & SONS LTD
JRC56706
0142-2421,
www.interscience.wiley.com,
https://publications.jrc.ec.europa.eu/repository/handle/JRC56706,
10.1002/sia.3297,
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