Lysozyme sorption in hydrogel contact lenses

Garrett, Q; Garrett, RW; Milthorpe, BK

Lysozyme sorption in hydrogel contact lenses

Garrett, Q Garrett, RW Milthorpe, BK

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Publication Type:: Journal Article
Citation:: Investigative Ophthalmology and Visual Science, 1999, 40 (5), pp. 897 - 903
Issue Date:: 1999-04-13

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Field	Value	Language
dc.contributor.author	Garrett, Q	en_US
dc.contributor.author	Garrett, RW	en_US
dc.contributor.author	Milthorpe, BK https://orcid.org/0000-0002-0867-9586	en_US
dc.date.issued	1999-04-13	en_US
dc.identifier.citation	Investigative Ophthalmology and Visual Science, 1999, 40 (5), pp. 897 - 903	en_US
dc.identifier.issn	0146-0404	en_US
dc.identifier.uri	http://hdl.handle.net/10453/9520
dc.description.abstract	PURPOSE. To examine the processes involved in formation of protein deposits on hydrogel contact lenses. METHODS. The adsorption and/or penetration of lysozyme on or into three types of contact lenses, etafilcon A, vifilcon A, and tefilcon, were investigated in vitro using a radiolabel- tracer technique, x-ray photoelectron spectroscopy, and laser scanning confocal microscopy. RESULTS. Binding of lysozyme to high-water-content, ionic contact lenses (etafilcon A and vifilcon A) was dominated by a penetration process. The extent of this penetration was a function of charge density of the lenses, so that there was a higher degree of penetration of lysozyme in etafilcon A than in vifilcon A lenses. In contrast, the binding of lysozyme to tefilcon lenses was a surface adsorption process. The adsorption and desorption kinetics showed similar trends to those found in human serum albumin (HSA) adsorption on lens surfaces. However, the extent of lysozyme adsorption on tefilcon is much higher than HSA adsorption, probably because of the self-association of lysozyme on the tefilcon lens surface. Furthermore, either penetration or adsorption of lysozyme involved reversible and irreversible processes and were both time dependent. CONCLUSIONS. Binding of lysozyme to hydrogel lenses involves surface adsorption or matrix penetration. These processes may be reversible or irreversible. The properties of the lens materials, such as charge density (ionicity) and porosity (water content) of the lenses, determine the type and rates of these processes.	en_US
dc.relation.ispartof	Investigative Ophthalmology and Visual Science	en_US
dc.subject.classification	Ophthalmology & Optometry	en_US
dc.subject.mesh	Hydrogel	en_US
dc.subject.mesh	Fluorescein-5-isothiocyanate	en_US
dc.subject.mesh	Muramidase	en_US
dc.subject.mesh	Microscopy, Confocal	en_US
dc.subject.mesh	Spectrometry, X-Ray Emission	en_US
dc.subject.mesh	Contact Lenses, Hydrophilic	en_US
dc.subject.mesh	Protein Binding	en_US
dc.subject.mesh	Kinetics	en_US
dc.subject.mesh	Adsorption	en_US
dc.subject.mesh	Time Factors	en_US
dc.subject.mesh	Hydrogel, Polyethylene Glycol Dimethacrylate	en_US
dc.title	Lysozyme sorption in hydrogel contact lenses	en_US
dc.type	Journal Article
utslib.citation.volume	5	en_US
utslib.citation.volume	40	en_US
utslib.for	1108 Medical Microbiology	en_US
utslib.for	06 Biological Sciences	en_US
utslib.for	11 Medical and Health Sciences	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - CHT - Health Technologies
utslib.copyright.status	closed_access
pubs.issue	5	en_US
pubs.publication-status	Published	en_US
pubs.volume	40	en_US

Abstract:

PURPOSE. To examine the processes involved in formation of protein deposits on hydrogel contact lenses. METHODS. The adsorption and/or penetration of lysozyme on or into three types of contact lenses, etafilcon A, vifilcon A, and tefilcon, were investigated in vitro using a radiolabel- tracer technique, x-ray photoelectron spectroscopy, and laser scanning confocal microscopy. RESULTS. Binding of lysozyme to high-water-content, ionic contact lenses (etafilcon A and vifilcon A) was dominated by a penetration process. The extent of this penetration was a function of charge density of the lenses, so that there was a higher degree of penetration of lysozyme in etafilcon A than in vifilcon A lenses. In contrast, the binding of lysozyme to tefilcon lenses was a surface adsorption process. The adsorption and desorption kinetics showed similar trends to those found in human serum albumin (HSA) adsorption on lens surfaces. However, the extent of lysozyme adsorption on tefilcon is much higher than HSA adsorption, probably because of the self-association of lysozyme on the tefilcon lens surface. Furthermore, either penetration or adsorption of lysozyme involved reversible and irreversible processes and were both time dependent. CONCLUSIONS. Binding of lysozyme to hydrogel lenses involves surface adsorption or matrix penetration. These processes may be reversible or irreversible. The properties of the lens materials, such as charge density (ionicity) and porosity (water content) of the lenses, determine the type and rates of these processes.

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http://hdl.handle.net/10453/9520