We studied the adsorption of bovine serum albumin (BSA) from phosphate-buffered saline (pH 7.4) to hydrophilic and hydrophobic surfaces. Attenuated total reflection Fourier transform infrared spectroscopy, supported by spectral simulation, allowed us to determine with high precision the amount of BSA adsorbed (surface coverage) and its structural composition. The adsorbed BSA molecules had an alpha-helical structure on both hydrophobic and hydrophilic surfaces but had different molecular conformations and adsorption strengths on the two types of surface. Adsorption of BSA was saturated at around 50% surface coverage on the hydrophobic surface, whereas on the hydrophilic surface the adsorption reached 95%. The BSA molecules adsorbed to the hydrophilic surface with a higher interaction strength than to the hydrophobic surface. Very little adsorbed BSA could be desorbed from the hydrophilic surface, even using 0.1 M sodium dodecyl sulfate, a strong detergent solution. The formation of BSA-phosphate surface complexes was observed under different BSA adsorption conditions on hydrophobic and hydrophilic surfaces. The formation of these complexes correlated with the more efficient blocking of nonspecific interactions by the adsorbed BSA layer. Results from the molecular modeling of BSA interactions with hydrophobic and hydrophilic surfaces support the spectroscopic findings.

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Exposure of protein-repelling oligo(ethylene glycol) (OEG) terminated alkanethiolate (AT) monolayers to ultraviolet (UV) light results in the damage of the OEG chains and photooxidation of the thiolate headgroups, which can be used for controlled tuning of protein-repelling properties within the so-called UV direct writing (UVDW) approach or for the preparation of mixed OEG-AT/specific-receptor films by so-called UV-promoted exchange reaction (UVPER). Using several model systems, we studied the effect of the wavelength (254–365 nm) on the course and efficiency of UVDW and UVPER applied to different OEG-AT matrices. The cross sections of the UV-induced damage were found to decrease significantly with increasing wavelength of UV light. In accordance with this behavior, the efficiencies of both UVDW and UVPER were maximal at a wavelength of 254 nm, somewhat lower at 313 nm, and lowest at 365 nm. Both UVDW and UVPER allowed a fine-tuning of protein affinity for nonspecific and specific adsorption, respectively, but UVDW did not occur below a certain, wavelength-dependent threshold dose. Performing UVPER below this dose enables us to suppress possible nonspecific adsorption of proteins even in the case of noncomplete exchange of the UV-damaged molecules of the primary OEG-AT matrix by receptor-bearing moieties. The obtained results are of direct relevance for the preparation of high-quality mixed OEG-AT/specific-receptor films and the fabrication of complex protein patterns by UVDW and UVPER lithography.