Adhesion of Lysozyme, Albumin and Transferrin to Two Types of FDA Group II Contact Lenses
Annual Meeting of the Federation of American Societies for Experimental Biology, Washington, DC, April 9-13, 2011
Tears contain ~60 different proteins that adhere to contact lenses, causing lens deterioration and ocular pathology. We examined the adhesion of three tear proteins to two different types of FDA Group II contact lenses (hilafilcon and omafilcon). Lenses were incubated in 2.0 mg/ml solutions of human lysozyme, albumin and transferrin for 1–4 days. Protein adhesion was determined by bicinchoninic acid assay. Lysozyme adhered to hilafilcon lenses in an up-down pattern, with a maximum on day 3. Lysozyme adhesion to omafilcon lenses was high after 1 day and remained high on day 4. Albumin adesion to both types of lenses was high after 1 day, declined, and increased on day 4. Transferrin adhesion to both lenses was initally low, increasing to a maximum on day 3 and declining on day 4. These results are due to differences in lens material and tear protein structure. Hilafilcon, more negatively charged than Omafilcon, absorbed more lysozyme (+ charged at physiological pH). Omafilcon lenses are coated with phosphorylcholine, reducing adhesion by the hydrophobic domains of albumin. Human apo-transferrin has few positive charges and thus bound more reluctantly to both materials.
Solanki, Darshan; Chandrasekaran, N.; Chodhry, R.; Cuprillnilson, S.; Desai, S.; Liberman, B.; Lee, V. S.; Lin, Y. J.; Nguyen, K.; Roughi, L.; Shah, S.; Sharma, V.; Thomas, P.; Janoff, Andrea; and Keith, Edward O., "Adhesion of Lysozyme, Albumin and Transferrin to Two Types of FDA Group II Contact Lenses" (2011). Oceanography Faculty Proceedings, Presentations, Speeches, Lectures. 368.