Lipid deposition on contact lenses in symptomatic and asymptomatic contact lens wearers.

PURPOSE: Lipid deposition on contact lenses (CL) has traditionally been believed to reduce comfort during CL wear. The purpose of this study was to quantify lipid deposition on CL in a group of symptomatic and asymptomatic adapted CL wearers. METHODS: This was a single-masked, randomized clinical trial. Only confirmed symptomatic (comfortable lens wear time (CWT) < 8 h and a noticeable reduction in comfort over the course of the day) and asymptomatic (CWT > 10 h and minimal reduction in comfort over the course of the day) participants were recruited to participate in the study. Participants wore senofilcon A lenses in combination with a polyquaternium-based care solution (OPTI-FREE Replenish). Worn CL samples were collected on Day 14. Deposited lipid amounts from the lenses (including cholesteryl ester, cholesterol and triolein) were quantified using a liquid chromatography-mass spectrometry technique. RESULTS: Lipid deposition was significantly higher in CL extracts of asymptomatic wearers compared to the symptomatic wearers for all lipid types quantified, including cholesteryl ester (2.1 ± 0.6 vs 1.6 ± 0.5 log µg/lens), cholesterol (1.5 ± 0.3 vs 1.1 ± 0.3 log µg/lens) and triolein (0.3 ± 0.2 vs 0.1 ± 0.1 log µg/lens) (all p < 0.002). The amount of cholesteryl ester deposited was greatest (p = 0.0001), followed by cholesterol, then triolein, for both the asymptomatic and symptomatic groups (both p = 0.0001). CONCLUSION: This study demonstrated that the asymptomatic group deposited a significantly greater amount of lipid on their CL. Although lipid levels measured are considered low to trigger any observable clinical deposition, they may influence other clinical outcomes, particularly comfort.

Kinetic Deposition of Polar and Non-polar Lipids on Silicone Hydrogel Contact Lenses.

Purpose: This study investigated kinetic lipid uptake to four silicone hydrogel (SiHy) lenses over a period of four weeks, using an in-vitro radiolabel method. Methods: Four contemporary monthly replacement SiHy lenses (lotrafilcon B, senofilcon C, comfilcon A, samfilcon A) were incubated in three different solutions: 1) An artificial tear solution (ATS) containing 14C-labeled phosphatidylcholine (PC), 2) an ATS containing 14C-cholesteryl oleate (CO) and 3) an ATS containing four 14C-radiolabeled lipids (PC, phosphatidylethanolamine, CO, and cholesterol (total lipid)). After 16 hours, lipids were extracted twice from the lenses with chloroform:methanol and the radioactive counts determined the lipid quantities to simulate 1 day of wear. OPTI-FREE PureMoist (Alcon) was used to clean and disinfect the remaining lenses daily and the lipid quantities were further determined after 2 weeks and 4 weeks. Results: The amount of total lipid increased for all lenses over time (p < .01). After four weeks, total lipid accumulated was 20.26 ± 0.15 µg/lens for senofilcon C, which was significantly higher (p < .01) than all other lens materials (samfilcon A - 17.84 ± 0.21; comfilcon A - 16.65 ± 0.12; lotrafilcon B - 7.41 ± 0.56 µg/lens). CO was highest on lotrafilcon B (1.26 ± 0.13 µg/lens) and senofilcon C attracted the most PC (3.95 ± 0.12 µg/lens) compared to the other materials. Conclusion: The amount of both polar and non-polar lipid deposition on monthly replacement SiHy lenses increased over 4 weeks, with significant differences being seen between lens materials.

Surface versus bulk activity of lysozyme deposited on hydrogel contact lens materials in vitro.

PURPOSE: To determine and compare the levels of surface versus bulk active lysozyme deposited on several commercially available hydrogel contact lens materials. METHODS: Hydrogel contact lens materials [polymacon, omafilcon A, nelfilcon A, nesofilcon A, ocufilcon and etafilcon A with polyvinylpyrrolidone (PVP)] were incubated in an artificial tear solution for 16 h. Total activity was determined using a standard turbidity assay. The surface activity of the deposited lysozyme was determined using a modified turbidity assay. The amount of active lysozyme present within the bulk of the lens material was calculated by determining the difference between the total and surface active lysozyme. RESULTS: The etafilcon A materials showed the highest amount of total lysozyme activity (519 ±â€¯8 µg/lens, average of Moist and Define), followed by the ocufilcon material (200 ±â€¯5 µg/lens) and these two were significantly different from each other (p < 0.05). The amount of surface active lysozyme on etafilcon and ocufilcon lens materials was significantly higher than that found on all other lenses (p < 0.05). There was no active lysozyme quantified in the bulk of the nelfilcon material, as all of the active lysozyme was found on the surface (1.7 ±â€¯0.3 µg/lens). In contrast, no active lysozyme was quantified on the surface of polymacon, with all of the active lysozyme found in the bulk of the lens material (0.6 ±â€¯0.6 µg/lens). CONCLUSIONS: The surface and bulk activity of lysozyme deposited on contact lenses is material dependent. Lysozyme deposited on ionic, high water content lens materials such as etafilcon A show significantly higher surface and bulk activity than many other hydrogel lens materials.

Biological and Clinical Implications of Lysozyme Deposition on Soft Contact Lenses.

Within a few minutes of wear, contact lenses become rapidly coated with a variety of tear film components, including proteins, lipids, and mucins. Tears have a rich and complex composition, allowing a wide range of interactions and competitive processes, with the first event observed at the interface between a contact lens and tear fluid being protein adsorption. Protein adsorption on hydrogel contact lenses is a complex process involving a variety of factors relating to both the protein in question and the lens material. Among tear proteins, lysozyme is a major protein that has both antibacterial and anti-inflammatory functions. Contact lens materials that have high ionicity and high water content have an increased affinity to accumulate lysozyme during wear, when compared with other soft lens materials, notably silicone hydrogel lenses. This review provides an overview of tear film proteins, with a specific focus on lysozyme, and examines various factors that influence protein deposition on contact lenses. In addition, the impact of lysozyme deposition on various ocular physiological responses and bacterial adhesion to lenses and the interaction of lysozyme with other tear proteins are reviewed. This comprehensive review suggests that deposition of lysozyme on contact lens materials may provide a number of beneficial effects during contact lens wear.

Protein deposition and its effect on bacterial adhesion to contact lenses.

PURPOSE: Bacterial adhesion to contact lenses is believed to be the initial step for the development of several adverse reactions that occur during lens wear such as microbial keratitis. This study examined the effect of combinations of proteins on the adhesion of bacteria to contact lenses. METHODS: Unworn balafilcon A and senofilcon A lenses were soaked in commercially available pure protein mixtures to achieve the same amount of various proteins as found ex vivo. These lenses were then exposed to Pseudomonas aeruginosa and Staphylococcus aureus. Following incubation, the numbers of P. aeruginosa or S. aureus that adhered to the lenses were measured. The possible effect of proteins on bacterial growth was investigated by incubating bacteria in medium containing protein. RESULTS: Although there was a significant (p < 0.003) increase in the total or viable counts of one strain of S. aureus (031) on balafilcon A lenses soaked in the lysozyme/lactoferrin combination, the protein adhered to lenses did not alter the adhesion of any other strains of P. aeruginosa or S. aureus (p > 0.05). Growth of S. aureus 031 (p < 0.0001) but not of P. aeruginosa 6294 was stimulated by addition of lysozyme/lactoferrin combination (2.8/0.5 mg/mL). Addition of lipocalin did not affect the growth of any strains tested (p > 0.05). CONCLUSIONS: Adsorption of amounts of lysozyme and lactoferrin or lipocalin equivalent to those extracted from worn contact lenses did not affect the adhesion of most strains of S. aureus or P. aeruginosa to lens surfaces.

Quantification of individual proteins in silicone hydrogel contact lens deposits.

PURPOSE: The aim of this study was to quantify specific proteins deposited on daily wear silicone hydrogel lenses used in combination with multipurpose disinfecting solutions (MPDSs) by applying multiple-reaction-monitoring mass spectrometry (MRM-MS). METHODS: Balafilcon A or senofilcon A contact lenses used with different MPDSs on a daily wear schedule were collected. Each worn lens was extracted and then digested with trypsin. MRM-MS was applied to quantify the amounts of lysozyme, lactoferrin, lipocalin-1, proline-rich protein-4, and keratin-1 in the extracts. RESULTS: The amount of protein extracted from the contact lenses was affected by the individual wearers, lens material, and type of care system used. Higher amounts of proteins were extracted from lenses after wear when they were used with an MPDS containing polyhexamethylene biguanide (PHMB) and poloxamer 407 compared with MPDSs containing polyquaternium-1 (PQ-1)/alexidine dihydrochloride with Tetronic 904 or PQ-1/ PHMB with poloxamine and sulfobetaine (p < 0.05). There was a correlation between the amount of lipocalin-1 or keratin-1 extracted from lenses and symptoms of ocular dryness. CONCLUSIONS: The MRM-MS technique is a promising approach that could be used to reveal associations of individual proteins deposited on lenses with performance of contact lenses during wear.

Quantification of protein deposits on silicone hydrogel materials using stable-isotopic labeling and multiple reaction monitoring.

This study was designed to use multiple reaction monitoring (MRM) for accurate quantification of contact lens protein deposits. Worn lenses used with a multipurpose disinfecting solution were collected after wear. Individual contact lenses were extracted and then digested with trypsin. MRM in conjunction with stable-isotope-labeled peptide standards was used for protein quantification. The results show that lysozyme was the major protein detected from both lens types. The amount of protein extracted from contact lenses was affected by the lens material. Except for keratin-1 (0.83 ± 0.61 vs 0.77 ± 0.20, p = 0.81) or proline rich protein-4 (0.11 ± 0.04 vs 0.15 ± 0.12, p = 0.97), the amounts of lysozyme, lactoferrin, or lipocalin-1 extracted from balafilcon A lenses (12.9 ± 9.01, 0.84 ± 0.50 or 2.06 ± 1.6, respectively) were significantly higher than that extracted from senofilcon A lenses (0.88 ± 0.13, 0.50 ± 0.10 or 0.27 ± 0.23, respectively) (p < 0.05). The amount of protein extracted from contact lenses was dependent on both the individual wearer and the contact lens material. This may have implications for the development of clinical responses during lens wear for different people and with different types of contact lenses. The use of MRM-MS is a powerful analytical tool for the quantification of specific proteins from single contact lenses after wear.