Protein adsorption on surfaces with grafted polymers: a theoretical approach.
A general theoretical framework for studying the adsorption of protein molecules on surfaces with grafted polymers is presented. The approach is a generalization of the single-chain mean-field theory, in which the grafted polymer-protein-solvent layer is assumed to be inhomogeneous in the direction perpendicular to the grafting surface. The theory enables the calculation of the adsorption isotherms of the protein as a function of the surface coverage of grafted polymers, concentration of protein in bulk, and type of solvent molecules. The potentials of mean force of the protein with the surface are calculated as a function of polymer surface coverage and amount of protein adsorbed. The theory is applied to model lysozyme on surfaces with grafted polyethylene oxide. The protein is modeled as spherical in solution, and it is assumed that the protein-polymer, protein-solvent, and polymer-solvent attractive interactions are all equal. Therefore, the interactions determining the structure of the layer (beyond the bare polymer-surface and protein-surface interactions) are purely repulsive. The bare surface-protein interaction is taken from atomistic calculations by Lee and Park. For surfaces that do not have preferential attractions with the grafted polymer segments, the adsorption isotherms of lysozyme are independent of the polymer length for chains with more than 50 ethylene oxide units. However, the potentials of mean force show strong variations with grafted polymer molecular weight. The competition between different conformations of the adsorbed protein is studied in detail. The adsorption isotherms change qualitatively for surfaces with attractive interactions with ethylene oxide monomers. The protein adsorption is a function of chain length--the longer the polymer the more effective it is in preventing protein adsorption. The structure of the layer and its deformation upon protein adsorption are very important in determining the adsorption isotherms and the potentials of mean force.
Szleifer
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I
Department of Chemistry, Purdue University, West Lafayette, Indiana 47907 USA. igal@shemesh.chem.purdue.edu
D000327:Adsorption; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D005027:Ethylene Oxide / Q000737:chemistry; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012997:Solvents / Q000737:chemistry; D013499:Surface Properties
D011108:Polymers; D011506:Proteins; D012997:Solvents; D009113:Muramidase; D005027:Ethylene Oxide