Protein Desorption Kinetics Depends on the Timescale of Observation

The presence of so-called reversible and irreversible protein adsorption on solid surfaces is well documented in the literature and represents the basis for the development of nanoparticles and implant materials to control interactions in physiological environments. Here, using a series of complementary single-molecule tracking approaches appropriate for different timescales, we show that protein desorption kinetics is much more complex than the traditional reversible-irreversible binary picture. Instead, we find that the surface residence time distribution of adsorbed proteins transitions from power law to exponential behavior when measured over a large range of timescales (10-2-106 s). A comparison with macroscopic results obtained using a quartz crystal microbalance suggested that macroscopic measurements have generally failed to observe such nonequilibrium phenomena because they are obscured by ensemble-averaging effects. These findings provide new insights into the complex phenomena associated with protein adsorption and desorption.

Automated summary

Using different timescales for single-molecule tracking, we discovered that the kinetics of protein desorption is more complex than previously thought. We observed a transition in the surface residence time distribution of adsorbed proteins from power law to exponential behavior over a large range of timescales. These findings provide new insights into the complexities of protein adsorption and desorption.