Microscale Diffusiophoresis of Proteins

Living systems are characterized by their spatially highly inhomogeneous nature which is susceptible to modify fundamentally the behavior of biomolecular species, including the proteins that underpin biological functionality in cells. Spatial gradients in chemical potential are known to lead to strong transport effects for colloidal particles, but their effect on molecular scale species such as proteins has remained largely unexplored. Here, we improve on existing diffusiophoresis microfluidic technique to measure protein diffusiophoresis in real space. The measurement of proteins is made possible by two ameliorations. First, a label-free microscope is used to suppress label interference. Second, improvements in numerical methods are developed to meet the particular challenges posed by small molecules. We demonstrate that individual proteins can undergo strong diffusiophoretic motion in salt gradients in a manner which is sufficient to overcome diffusion and which leads to dramatic changes in their spatial organization on the scale of a cell. Moreover, we demonstrate that this phenomenon can be used to control the motion of proteins in microfluidic devices. These results open up a path towards a physical understanding of the role of gradients in living systems in the spatial organization of macromolecules and highlight novel routes towards protein sorting applications on device.

Automated summary

Living systems are highly spatially inhomogeneous, which can fundamentally change the behavior of biomolecular species, including proteins. In this study, an improved diffusiophoresis microfluidic technique was used to measure protein diffusiophoresis in real space. Individual proteins were found to undergo strong diffusiophoretic motion in salt gradients, leading to significant changes in their spatial organization. This phenomenon can also be used to control protein motion in microfluidic devices.