Abstract
A hydrophobicity gradient was created by gradually exposing a polydimethylsiloxane film to a radio frequency glow discharge in an oxygen atmosphere. A change in contact angle from 100 to 0° was measured along the gradient surface by means of the Wilhelmy balance technique. The gradient surface was characterized by studying the adsorption from single protein solutions of human albumin, IgG and fibrinogen using total internal reflectance fluorescence (TIRF). Generally, adsorption values similar to monolayer capacities were measured on the hydrophobic side. The adsorption decreased towards the hydrophilic end in correspondence with the change in contact angle. The displacement of proteins with a ethylene oxide-propylene oxide copolymer (EO 70PO 100EO 70) was higher on the hydrophobic side than on the hydrophilic side. Albumin showed an adsorption peak in the wetting transition region, indicating a very strong affinity.
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