AVS 52nd International Symposium
    Biomaterial Interfaces Wednesday Sessions
       Session BI1-WeM

Paper BI1-WeM8
Protein Nanopatterning onto Nanostructured Polymer Surfaces

Wednesday, November 2, 2005, 10:40 am, Room 311

Session: Protein-Surface Interactions
Presenter: C. Satriano, University of Catania, Italy
Authors: C. Satriano, University of Catania, Italy
G.M.L. Messina, University of Catania, Italy
G. Marletta, University of Catania, Italy
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The preferential adsorption of human fibronectin, lactoferrin, serum albumin and lysozime has been investigated onto nanostructured polysiloxane surfaces obtained by a colloidal crystal-based technique in combination with cold plasma treatment. In particular, 2D arrays of nanopores, having typical dimensions of about 55 nm of diameter and about 3 nm and 1 nm respectively for the rim height and the pore depth were fabricated. Polystyrene nanoparticles were used to imprint regularly-spaced nanopores within a bilayer formed by an untreated polysiloxane film onto a plasma-modified one. The internal area of the pores consisted of hydrophilic O@sub 2@-plasma treated polysiloxane, while the external surface was the hydrophobic untreated polymer. The spatially-resolved features of adsorbed proteins were investigated by means of Atomic Force Microscopy. The in situ adsorption process on homogeneously modified surfaces has been investigated by means of Quartz Crystal Microbalance with Dissipation Monitoring, while X-ray Photoelectron Spectroscopy was employed to evaluate ex-situ the coverage and thickness of the protein adlayers for the two types of surfaces. The results showed that the relevant chemical factors are the surface free energy and the chemical termination of the different surfaces. In particular, human fibronectin and lactoferrin showed a preferential adsorption outside of the hydrophilic nanopores, while lysozime and human serum albumin seem prefer the nanopore area. The results suggest that it could be possible to achieve the separation of protein mixtures by a spatially resolved adsorption.