Protein—surface interactions in the presence of polyethylene oxide

Abstract The protein resistance character of polyethylene oxide (PEO) chains terminally attached to a hydrophobic solid substrate is theoretically studied. Steric repulsion, van der Waals attraction, and hydrophobic interaction free energies are considered. The results are dependent on the chain length and surface density of PEO. The protein approaches the PEO surface by diffusion and is affected by the van der Waals attraction between the PEO surface and protein through water. Further approach of the protein initiates the compression of PEO chains, which induces a steric repulsion effect; an additional van der Waals attraction becomes important between the substrate and protein through the water solvated PEO layer. The van der Waals component with the substrate decreases with increasing surface density and chain length of terminally attached PEO chains. Other synthetic polymers were also studied, indicating that the protein resistance character is related to the refractive index, with PEO having the lowest refractive index of the common water-soluble synthetic polymers. The osmotic and elastic constants of steric repulsion for terminally attached PEO were estimated as ∼0.007 and 0.02, respectively, from literature data for PEO adsorbed to mica. The steric repulsion free energy and the combined steric repulsion and hydrophobic interaction free energies were calculated as a function of surface density and chain length of PEO. The free energy calculations as a function of surface density and chain length of PEO reveal that a high surface density and long chain length of terminally attached PEO should exhibit optimal protein resistance, with the attainment of high surface density of PEO being more important than long chain length. These theoretical results should be helpful in the design and development of materials resistant to protein adsorption.

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