Abstract
Lacrimal glands adjacent to the eye secrete tear proteins that deposit onto contact lenses. In order to study this process, three types of FDA group II contact lenses fabricated from hilafilcon, omafilcon and tisifilcon A were incubated in 2.0 mg/mL solutions of holo-transferrin for 1, 2, 3 and 4 days. The degree of protein adhesion was determined by bicinchoninic acid assay. Transferrin adhered to hilafilcon contact lenses in an increasing pattern from day 1 to day 3, with a decrease on day 4. Transferrin adhesion to omafilcon contact lenses followed the same trend with greater protein adhesion than the hilafilcon lenses. Transferrin adhesion to tisifilcon A contact lenses increased on days 1 and 2, and then decreased on day 3, and increased again on day four. These differences in transferrin adhesion may be associated with the inherent positive charge on its N-terminus and positively charged arginine residues in the protein, but other factors must be important because the hilafilcon material is more negatively charged than the omafilcon material, leading one to expect that transferrin should bind to a greater degree to hilafilcon than to omafilcon, in contrast to my results.
Faculty Sponsors
Dr. Andrea Janoff, Dr. Edward O. Keith
Project Type
Event
Location
Alvin Sherman Library
Start Date
4-13-2012 1:00 PM
End Date
4-13-2012 5:30 PM
Examining Relationships of Transferrin Adhesion to Hilafilcon, Omafilcon, and Tisifilcon A Contact Lenses
Alvin Sherman Library
Lacrimal glands adjacent to the eye secrete tear proteins that deposit onto contact lenses. In order to study this process, three types of FDA group II contact lenses fabricated from hilafilcon, omafilcon and tisifilcon A were incubated in 2.0 mg/mL solutions of holo-transferrin for 1, 2, 3 and 4 days. The degree of protein adhesion was determined by bicinchoninic acid assay. Transferrin adhered to hilafilcon contact lenses in an increasing pattern from day 1 to day 3, with a decrease on day 4. Transferrin adhesion to omafilcon contact lenses followed the same trend with greater protein adhesion than the hilafilcon lenses. Transferrin adhesion to tisifilcon A contact lenses increased on days 1 and 2, and then decreased on day 3, and increased again on day four. These differences in transferrin adhesion may be associated with the inherent positive charge on its N-terminus and positively charged arginine residues in the protein, but other factors must be important because the hilafilcon material is more negatively charged than the omafilcon material, leading one to expect that transferrin should bind to a greater degree to hilafilcon than to omafilcon, in contrast to my results.
