Influence of contact lens material surface characteristics and replacement frequency on protein and lipid deposition.
The aim of the study was to quantify the influence of both contact lens material and replacement frequency on protein and lipid deposition. The following hypotheses were tested: (1) both protein and lipid interaction with contact lenses are material-dependent, and (2) the key factors are the material ionicity for the protein deposition and the material chemical composition for the lipid deposition. Three high water content contact lens materials were tested: netrafilcon A (FDA group II, Gentle Touch), etafilcon A (FDA group IV, Acuvue), and vifilcon A (FDA group IV, Focus). Contact lens spoilation was analyzed using ultraviolet spectroscopy and fluorescence spectrophotometry. The results showed that (1) significantly more proteins were deposited on the ionic materials than on the nonionic materials, and that among the ionic materials, the higher the ionicity, the higher the level of protein deposition; (2) there were significantly more surface proteins on the ionic materials after 3 months than after 1 month of wear, but no difference over time was demonstrated for the nonionic materials; and (3) significantly more lipids were deposited onto the surface of vifilcon A than etafilcon A or netrafilcon A, and the presence of vinylpyrrolidone in the vifilcon A formulation was thought to be the cause of increased deposition. The protein and lipid interactions with contact lenses were found to be material- and time-dependent. Protein attraction was found to be related to the material ionicity. The presence of vinylpyrrolidone was a key factor in the attraction of lipids.
Aston Biomaterials Research Unit, CEAC, Aston University, Birmingham, United Kingdom.
C
C
Maïssa
V
V
Franklin
M
M
Guillon
B
B
Tighe
D003263:Contact Lenses, Hydrophilic; D004209:Disposable Equipment; D005136:Eye Proteins / Q000378:metabolism*; D005260:Female; D006801:Humans; D050356:Lipid Metabolism; D008297:Male; D011108:Polymers; D011485:Protein Binding; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013997:Time Factors
D005136:Eye Proteins; D011108:Polymers; C042434:tear proteins