No abstract

The hydrophobic nature of rigid gas-permeable contact lenses causes them to be more prone to lipid than to protein deposition. When both types of molecule are present in an artificial tear solution, the hydrophobic sites of the lipid molecules are attracted to the lens matrix while the more hydrophilic sites are repelled by the matrix and, thereby, exposed to the aqueous surroundings. Thus, lipid binding to rigid gas-permeable contact lenses reduces the hydrophobicity of the lens surface allowing protein to bind. The bound deposited hydrophilic protein then alters subsequent binding of both protein and lipid.

Protein adsorption on a group IV lens renders the lens surface less hydrophilic and, thereby, more susceptible to lipid deposition, which in turn increases surface hydrophobicity and inhibits additional protein deposition. For a group II lens, positively charged protein competes with and replaces some of the polar lipids attached to the lens. Thus, the interaction of protein and lipid on a lens surface most prone to a particular contaminant apparently makes it less likely for that contaminant to bind.

No abstract

No abstract