Solid–liquid interfacial energy as a tool to estimate shifts in isoelectric points of adsorbed proteins on solid surfaces

This work reports the estimation of isoelectric points (pIs) of adsorbed amino acids and proteins on solid surfaces in the pH range between 3.5–11.0 from a measurement of solid/liquid interfacial energy. The values thus obtained are compared with the pIs determined in solution phase by other methods. Both glass and Teflon have been chosen as model solid surfaces. Close agreement between the reference pI values, obtained by the capillary isoelectric focusing and those obtained at solid/liquid interface is observed within an average difference of 0.04–0.08 pH unit when the pIs are above the pI of glass. For systems whose pIs are far away from that of glass (either in the acidic or highly alkaline range), a large shift in the isoelectric point is observed. In case of Teflon the pIs are closer to the reported values than at glass/liquid interface. This could be due to the fact that Teflon being a hydrophobic surface, its surface is dominated by dispersive forces, which may not be seriously affected by pH changes. The shift in the values at solid/liquid interface compared to that in solution have been examined using an ‘image charge approach.’

This work reports the estimation of isoelectric points (pIs) of adsorbed amino acids and proteins on solid surfaces in the pH range 3.5–11.0 from a measurement of solid/liquid interfacial energy. Close agreement between the reference pI values obtained by the capillary isoelectric focusing and those obtained at solid/liquid interface is observed within an average difference of 0.04–0.08 pH unit when the pIs are above the pI of glass. For systems whose pIs are far away from that of glass (either in the acidic or highly alkaline range), a large shift in the isoelectric point is observed. In case of Teflon the pIs are closer to the reported values than at glass/liquid interface.Figure optionsDownload as PowerPoint slide