Title

Adhesion of Transferrin and Albumin to FDA Group II Omafilcon Contact Lenses

Event Name/Location

6th International Conference on the Tear Film & Ocular Surface: Basic Science and Clinical Relevance, Florence, Italy, September 22-25, 2010

Document Type

Poster

Publication Date

9-24-2010

Abstract

Objective:Tear protein deposits on contact lenses can cause irritation of the conjunctiva and are associated with bacterial infection. The adhesion of transferrin and albumin to Omafilcon contact lenses was investigated. The charges on protein molecules interact with the contact lens hydrogel polymer causing adhesion of the proteins to the lenses. Methods: Lenses were incubated for 5 days in a solution (2 mg/mL) of each protein. Bicinchoninic acid colorimetry was performed to determine protein concentration in the vials and protein adhesion to lenses. Results: The albumin concentration in the incubation vials remained fairly constant while the concentration of transferrin in the vials fluctuated. Albumin initially adhered to the lenses, declined slightly on subsequent days, and increased again on day five. Transferrin adhered to the lenses consistently, reaching peak deposition after four days of incubation, before declining on day five. The adhesion of transferrin to the Omafilcon lenses was similar to the adhesion of transferrin to Hilafilcon lenses (both FDA Group II:

nonionic high water). Albumin adhesion to Omafilcon contact lenses resembled the adhesion of lysozyme to the same lenses. Conclusion: Human serum albumin has three domains that allows albumin to bind and release hydrophobic molecules while transferrin has numerous positive charges. Thus, the negatively charged hydrophilic polymer of the Omafilcon lenses facilitated transferrin adhesion but limited albumin adhesion. Supported by a NSU President’s Fac

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