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Deposited proteins on contact lens surfaces refer to the accumulation of tear film-derived proteins, such as lysozyme, lactoferrin, and albumin, onto the surface and within the matrix of contact lenses during wear (Luensmann & Jones, 2012). While these proteins are essential components of the innate immune system in the tear film, their adsorption onto synthetic lens polymers often leads to conformational changes and denaturation (Omali et al., 2015). Denatured proteins are recognized as foreign by the ocular immune system, potentially triggering inflammatory responses such as giant papillary conjunctivitis (GPC) and contact lens-induced acute red eye (CLARE) (Stapleton et al., 2008). Furthermore, these deposits can serve as a biological scaffold for bacterial adhesion, significantly increasing the risk of microbial keratitis (Subbaraman et al., 2006). Management of these deposits typically involves the use of multi-purpose solutions containing surfactants or specialized enzymatic cleaners, such as papain and subtilisin, which hydrolyze the proteins into smaller, soluble fragments for removal (Fowler et al., 1984). Understanding the kinetics of these deposits is vital for the development of next-generation biomaterials with improved anti-fouling properties.
Proteolytic cleavage of peptide bonds in adsorbed proteins to facilitate removal from the lens surface; surfactant-mediated emulsification and displacement; oxidative denaturation and solubilization.
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