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    Adsorption of Fibronectin, Fibrinogen, and Albumin on TiO2: Time-Resolved Kinetics, Structural Changes, and Competition Study

    Year: 2012

    Journal: BIOINTERPHASES Volume 7, Numbers 1-4 (2012), 48, DOI: 10.1007/s13758-012-0048-4, 20120922

    Authors: Marta Pegueroles, Chiara Tonda-Turo, Josep A. Planell, Francisco-Javier Gil and Conrado Aparicio

    Last authors: Conrado Aparicio

    Organizations: Biomaterials, Biomechanics, and Tissue Engineering Group, Department of Material Science and Metallurgy, Technical University of Catalonia, Av. Diagonal 647, 08028 Barcelona, Spain e-mail: marta.pegueroles@upc.edu C. Tonda-Turo e-mail: chiara.tondaturo@polito.it J. A. Planell e-mail: japlanell@ibec.pcb.ub.es; josep.a.planell@upc.edu F.-J. Gil e-mail: francesc.xavier.gil@upc.edu M. Pegueroles

    Country: spain

    An understanding of protein adsorption process is crucial for designing biomaterial surfaces. In this work, with the use of a quartz-crystal microbalance with dissipation monitoring, we researched the following: (a) the kinetics of adsorption on TiO2 surfaces of three extensively described proteins that are relevant for metallic implant integration [i.e., albumin (BSA), fibrinogen (Fbg), and fibronectin (Fn)]; and (b) the competition of those proteins for adsorbing on TiO2 in a two-step experiment consisted of sequentially exposing the surfaces to different monoprotein solutions. Each protein showed a different process of adsorption and properties of the adlayer—calculated using the Voigt model. The competition experiments showed that BSA displaced larger proteins such as Fn and Fbg when BSA was introduced as the second protein in the system, whereas the larger proteins laid on top of BSA forming an adsorbed protein bi-layer when those were introduced secondly in the system.