Mass spectrometry-based proteomic analyses of contact lens deposition

The purpose of this report is to describe the contact lens deposition proteome associated with two silicone hydrogel contact lenses and care solutions using a mass spectrometric-based approach.

This was a randomized, controlled, examiner-masked crossover clinical trial that included 48 participants. Lenses and no-rub care solutions evaluated included galyfilcon A (Acuvue Advance, Vistakon Inc., Jacksonville, FL), lotrafilcon B (O2 Optix, CIBA Vision Inc., Duluth, GA), AQuify (CIBA Vision Inc.), and ReNu MoistureLoc (Bausch and Lomb Inc., Rochester, NY). After two weeks of daily wear in each lens-solution combination, the left lens was removed by the examiner (using gloves and forceps) and placed in a protein precipitation buffer (acetone). The precipitate was quantitated for total protein concentration (per lens), and proteins were then identified using liquid chromatography tandem mass spectrometry (nano-LC-MS/MS) and peptide sequencing.

Between 7.32 and 9.76 microg/lens of protein was observed on average from each lens-solution combination. There were 19 total unique proteins identified across the two lens materials, and six proteins were identified in all four lens-solution combinations including lipocalin, lysozyme, lacritin, lactoferrin, proline rich 4, and Ig Alpha. Lotrafilcon B was associated with 15 individual proteins (across both care solutions), and 53% of these proteins were observed in at least 50% of the analyses. Galyfilcon A was associated with 13 individual proteins, and 38.5% of these proteins were observed in at least 50% of the analyses. There were three unique proteins identified from galyfilcon A and four unique proteins identified from lotrafilcon B.

The total amount of proteins identified from silicone hydrogel materials is much less than the amount from traditional soft lens materials. For the most part, the deposition proteome across these lenses is similar, although the different polymer characteristics might be associated with some variability in observance of the less frequently identified proteins.