Total removal of intact blood plasma proteins deposited on surface-grafted polymer brushes

Nonspecific protein adsorption, referred to as fouling, is a major clinical problem accompanying any material coming into direct contact with biological fluids, especially blood/plasma. Not only is protein fouling detrimental per se but it also promotes platelet adhesion, the initiation of blood coagulation, and/or complement activation. In spite of efforts to develop novel surfaces which suppress protein fouling, still only little is known about the mechanisms behind protein fouling from blood and other complex biological media. In order to unravel the mechanisms, precise identification of the proteins that foul the surface is necessary. This is particularly challenging for those surfaces with reduced protein fouling, such as polymer brushes. This report introduces a route to analyze the proteins by mass spectrometry using an optimized protocol. We demonstrate proteomics-compatible buffers/solutions suitable for desorption of adsorbed proteins on low fouling polymer brushes. In this way, not only mass spectrometry, but also a plethora of other studies based on state-of-the-art proteomics can be accessed. Buffers/solutions suitable for total desorption of adsorbed proteins on low fouling polymer brushes are presented, enabling analysis not only by MS, but also a plethora of other state-of-the-art proteomics methods.