This is U0126 most probably due to an insufficient amount of proteins, which is a direct result of the low number of nanowires available. In contrast, the fluorescence method presented here requires only a few mm2 for each sample and might be used for other nanoparticles that are too expensive to produce in big quantities. We have used a fluorescence microscopy method to measure the relative amount of laminin adsorbed on GaP nanowires compared to flat GaP surface. Laminin adsorbs up

to 4 times more on 55 nm diameter nanowires, when normalized to the surface area, compared to the flat surface. We showed that this phenomenon is neither due to electrostatic effects, nor crystalline effects but may be attributed to purely geometric effects, with small-diameter nanowires having more adsorbed laminin per surface area compared to nanowires with larger diameters. Preferential adsorption of the ECM protein laminin to nanowires may be part of the explanation why nanowire substrates

are beneficial for cell attachment and growth. The authors would like to thank Gaëlle Piret and Martina Schneider for help with the spectrophotometer and Tommy Cedervall for help with the polyacrylamide gels. This work was performed at the Microscopy Facility at the Department of Biology, Lund University. This work was funded by the Swedish research council (VR) and the Nanometer Structure Consortium at Lund University (nmC@LU). “
“Stainless steel is widely used in biological environments, for example as implant materials [1] or in food contact applications mTOR inhibitor [2] and [3]. Such

environments inevitably result in the adsorption of proteins that can significantly influence the surface oxide characteristics and enhance the release of metals, even if stainless steel is in its passive state (not actively corroding) and maintains a high corrosion resistance [4]. The surface oxide (“passive film”) of all stainless steel grades is mainly composed of iron(III) and chromium(III) oxides and is typically 2–5 nm thick in most acidic and neutral environments at room temperature with no applied potential [4], [5], [6] and [7]. The relative proportion of chromium (Cr) to iron (Fe) in the surface oxide is not necessarily altered upon contact with neutral non-complexing aqueous solutions [4] and [7]. It is, however, strongly affected (enhanced Loperamide proportion of Cr) in acidic, complexing (chelating), and/or protein-containing solutions, such as citric acid/citrate [6], [8] and [9], nitric acid [6], sulfuric acid [7] and [10], and solutions containing bovine serum albumin (BSA) [4]. The surface oxide of stainless steel is in complexing environments exposed to different ligands (complexing agents) such as citrate and proteins. This induces ligand adsorption, complexation with a surface oxide/hydroxide metal atom, and the possible detachment of the ligand–metal complex from the surface oxide (rate limiting step) [11].