| The dynamics of protein adsorption plays a crucial role in determining the biocompatibility of biomaterials. Large scale analysis of protein adsorption on the surfaces of biomaterials was performed using proteomics. It was found that proteomic analysis allowed the identification of a number of adsorbed serum/plasma proteins on surfaces, especially serum amyloid P, and could be used to measure the relative amounts of proteins adsorbed to the surface. We determined the identity of serum or plasma proteins that displaced adsorbed bovine serum albumin. We found that serum amyloid P has a high affinity for the surfaces of hydrophobic biomaterials, such as polyethylene terephthalate (PET) and silicone rubber (PDMS), and serum amyloid P can promote leukocyte adhesion to these surfaces.; Conformation and orientation of adsorbed proteins are important factors that ultimately determine the biocompatibility of materials. We developed an experimental technique to determine the extent and the rate of the conformational change of adsorbed proteins. Using Hydrogen/Deuterium (H/D) exchange, we demonstrated a method that allows us to measure the extent of conformational changes of adsorbed proteins, which may eventually be useful in determining appropriate rate constants that describe this process.; To control protein adsorption on biomaterials, we developed a surface coating method to reduce protein adsorption and cell adhesion, using a layer-by-layer method. We fabricated a biocompatible, thin and dense surface film by sequential reaction between vinyl sulfone groups and thiols or amines. Using proteomics, we found that an increase in the number of polyethylene glycol (PEG) layers leads to a substantial reduction in the amount of protein adsorption and cell adhesion. It was also found that endothelial cell adhesion and spreading could be restored by attaching RGD containing peptides on the PEG film. |
