Effect of the interplay between protein and surface on the properties of adsorbed protein layers.

Although protein adsorption to surface is a common phenomenon, investigation of the process is challenging due to the complexity of the interplay between external factors, protein and surface properties. Therefore experimental approaches have to measure the properties of adsorbed protein layers with high accuracy in order to achieve a comprehensive description of the process. To this end, we used a combination of two biosensing techniques, dual polarization interferometry and quartz crystal microbalance with dissipation. From this, we are able to extract surface coverage values, layer structural parameters, water content and viscoelastic properties to examine the properties of protein layers formed at the liquid/solid interface. Layer parameters were examined upon adsorption of proteins of varying size and structural properties, on surfaces with opposite polarity. We show that "soft" proteins such as unfolded α-synuclein and high molecular weight albumin are highly influenced by the surface polarity, as they form a highly diffuse and hydrated layer on the hydrophilic silica surface as opposed to the denser, less hydrated layer formed on a hydrophobic methylated surface. These layer properties are a result of different orientations and packing of the proteins. By contrast, lysozyme is barely influenced by the surface polarity due to its intrinsic structural stability. Interestingly, we show that for a similar molecular weight, the unfolded α-synuclein forms a layer with the highest percentage of solvation not related to surface coverage but resulting from the highest water content trapped within the protein. Together, these data reveal a trend in layer properties highlighting the importance of the interplay between protein and surface for the design of biomaterials.

Effect of the interplay between protein and surface on the properties of adsorbed protein layers

Although protein adsorption to surface is a common phenomenon, investigation of the process is challenging due to the complexity of the interplay between external factors, protein and surface properties. Therefore experimental approaches have to measure the properties of adsorbed protein layers with high accuracy in order to achieve a comprehensive description of the process. To this end, we used a combination of two biosensing techniques, dual polarization interferometry and quartz crystal microbalance with dissipation. From this, we are able to extract surface coverage values, layer structural parameters, water content and viscoelastic properties to examine the properties of protein layers formed at the liquid/solid interface. Layer parameters were examined upon adsorption of proteins of varying size and structural properties, on surfaces with opposite polarity. We show that "soft" proteins such as unfolded α-synuclein and high molecular weight albumin are highly influenced by the surface polarity, as they form a highly diffuse and hydrated layer on the hydrophilic silica surface as opposed to the denser, less hydrated layer formed on a hydrophobic methylated surface. These layer properties are a result of different orientations and packing of the proteins. By contrast, lysozyme is barely influenced by the surface polarity due to its intrinsic structural stability. Interestingly, we show that for a similar molecular weight, the unfolded α-synuclein forms a layer with the highest percentage of solvation not related to surface coverage but resulting from the highest water content trapped within the protein. Together, these data reveal a trend in layer properties highlighting the importance of the interplay between protein and surface for the design of biomaterials. © 2014 The Authors.

Altering the ordering and disordering of a triangular nanographene at room temperature.

Molecular self-organization has the potential to serve as an efficient and versatile tool for the spontaneous creation of low-dimensional nanostructures on surfaces. We demonstrate how the subtle balance between intermolecular interactions and molecule-surface interactions can be altered by modifying the environment or through manipulation by means of the tip in a scanning tunnelling microscope (STM) at room temperature. We show how this leads to the distinctive ordering and disordering of a triangular nanographene molecule, the trizigzag-hexa-peri-hexabenzocoronenes-phenyl-6 (trizigzagHBC-Ph6), on two different surfaces: graphite and Au(111). The assembly of submonolayer films on graphite reveals a sixfold packing symmetry under UHV conditions, whereas at the graphite-phenyloctane interface, they reorganize into a fourfold packing symmetry, mediated by the solvent molecules. On Au(111) under UHV conditions in the multilayer films we investigated, although disorder prevails with the molecules being randomly distributed, their packing behaviour can be altered by the scanning motion of the tip. The asymmetric diode-like current-voltage characteristics of the molecules are retained when deposited on both substrates. This paper highlights the importance of the surrounding medium and any external stimulus in influencing the molecular organization process, and offers a unique approach for controlling the assembly of molecules at a desired location on a substrate.