The adsorption behavior of BSA protein on amphiphilic PEG-PS membrane

Revealing the adsorption behavior of proteins on amphiphilic polymers is an interesting study. For the first time, the adsorption behavior of bovine serum albumin (BSA) protein on the surface of polyethylene glycol polystyrene (PEG-PS) amphiphilic polymer membrane is developed by molecular dynamics (MD) simulations and experiments. We found that PEG-PS has the ability to resist BSA protein adsorption. The adsorption of BSA on its surface undergoes a process of "rotation-preadsorption-desorption-final adsorption". After adsorption, the helical structure of BSA underwent "tight-loose-unwinding" changes. The transition from PEG chain helical structure to free coil structure is a key factor leading to the adsorption and desorption of BSA. Furthermore, the hydrophobic force of PS is the main driving force for BSA adsorption. These studies can inspire the design of amphiphilic materials to realize protein antifouling or transportation materials.