In this work, the electrografting of Al-7075 aluminium alloy substrates with 4-nitrobenzenediazonium salt (4-NBD) films was studied on a complex aluminium alloy surface. Prior to the electrografting reaction, the substrates were submitted to different surface treatments to modify the native aluminium oxide layer and unveil intermetallic particles (IMPs). The formation of the 4-NBD films could be correlated with the passive film state and the distribution of IMPs. The corresponding electrografting reaction was performed by cyclic voltammetry which allowed the simultaneous analysis of the redox reaction by a number of complementary surface-analytical techniques. Spatially resolved thin film analysis was performed by means of SEM-EDX, AFM, PM-IRRAS, Raman spectroscopy, XPS, and SKPFM. The collected data show that the 4-NBD film is preferentially formed either on the Al oxide layer or the IMP surface depending on the applied potential range. Potentials between −0.1 and −1.0 VAg/AgCl mostly generated nitrophenylene films on the oxide covered aluminium, while grafting between −0.1 and −0.4 VAg/AgCl favours the growth of these films on IMPs.

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Multiprotein adsorption from complex body fluids represents a highly important and complicated phenomenon in medicine. In this work, multiprotein adsorption from diluted human serum at gold and oxidized iron surfaces is investigated at different serum concentrations and pH values. Adsorption-induced changes in surface topography and the total amount of adsorbed proteins are quantified by atomic force microscopy (AFM) and polarization-modulation infrared reflection absorption spectroscopy (PM-IRRAS), respectively. For both surfaces, stronger protein adsorption is observed at pH 6 compared to pH 7 and pH 8. PM-IRRAS furthermore provides some qualitative insights into the pH-dependent alterations in the composition of the adsorbed multiprotein films. Changes in the amide II/amide I band area ratio and in particular side-chain IR absorption suggest that the increased adsorption at pH 6 is accompanied by a change in protein film composition. Presumably, this is mostly driven by the adsorption of human serum albumin, which at pH 6 adsorbs more readily and thereby replaces other proteins with lower surface affinities in the resulting multiprotein film.