Abstract: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.
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