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Updated: Apr 12, 2026
06:29
Effect of Artificial Tear Formulations on the Metabolic Activity of Human Corneal Epithelial Cells after Exposure to Desiccation
Published on: May 2, 2020
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Competitive Effects from an Artificial Tear Solution to Protein Adsorption.
Brad Hall1, Lyndon W Jones, James A Forrest
1*PhD †PhD, FCOptom, FAAO Centre for Contact Lens Research, School of Optometry and Vision Science (all authors), and Department of Physics and Astronomy and Guelph-Waterloo Physics Institute (LWJ, JAF), University of Waterloo, Waterloo, Ontario, Canada.
Summary
Protein adsorption to contact lenses varies by material and artificial tear solution (ATS) components. Some lens materials show competitive adsorption and reversible protein binding, impacting lens performance.
Area of Science:
- Ophthalmology
- Biomaterials Science
- Surface Chemistry
Background:
- Protein adsorption onto contact lenses is a key factor influencing lens performance and wearer comfort.
- Understanding protein-material interactions is crucial for developing advanced contact lens materials.
Purpose of the Study:
- To compare lysozyme, lactoferrin, and albumin adsorption on various contact lens materials.
- To differentiate between single-protein solutions and multicomponent artificial tear solutions (ATS).
- To distinguish between loosely and tightly bound proteins, including denatured forms.
Main Methods:
- Time-dependent protein adsorption measurements over 1 minute to 1 week.
- Used radiolabeling to quantify lysozyme, lactoferrin, and albumin.
- Investigated protein binding in both ATS and buffered saline, distinguishing reversible and irreversible binding.
Main Results:
- Lotrafilcon B showed rapid competitive adsorption of all tested proteins within 1 minute.
- Ionic materials (balafilcon A, etafilcon A) exhibited significant reversible binding of lysozyme and lactoferrin within 10 minutes.
- Senofilcon A showed minimal detectable protein deposition within the study's confidence thresholds.
Conclusions:
- Protein adsorption and binding reversibility are highly dependent on the specific contact lens material.
- Coadsorption with ATS components can enhance the reversibility of protein binding to contact lenses.
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