In vitro adsorption of tear proteins to hydroxyethyl methacrylate-based contact lens materials

Carney, FP; Morris, CA; Milthorpe, B; Flanagan, JL; Willcox, MDP

In vitro adsorption of tear proteins to hydroxyethyl methacrylate-based contact lens materials

Carney, FP Morris, CA Milthorpe, B

Flanagan, JL Willcox, MDP

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Publication Type:: Journal Article
Citation:: Eye and Contact Lens, 2009, 35 (6), pp. 320 - 328
Issue Date:: 2009-11-01

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Field	Value	Language
dc.contributor.author	Carney, FP	en_US
dc.contributor.author	Morris, CA	en_US
dc.contributor.author	Milthorpe, B https://orcid.org/0000-0002-0867-9586	en_US
dc.contributor.author	Flanagan, JL	en_US
dc.contributor.author	Willcox, MDP	en_US
dc.date.issued	2009-11-01	en_US
dc.identifier.citation	Eye and Contact Lens, 2009, 35 (6), pp. 320 - 328	en_US
dc.identifier.issn	1542-2321	en_US
dc.identifier.uri	http://hdl.handle.net/10453/10561
dc.description.abstract	Objectives: Investigations of polymer interactions in single protein solutions is a necessary step in the elucidation of in vivo early binding events during protein deposition on hydroxyethyl methacrylate-based contact lens materials. Quantity and tenacity of binding of significant tear components to groups I and IV contact lenses was assessed. Competitive binding by these components was also examined. Methods: Adsorption on FDA groups I and IV hydrogel lenses was monitored using I-labeled protein. Lenses were incubated in increasing concentrations of radiolabeled single species proteins in solution. For competition experiments, concentration of each radiolabeled protein was held constant and the adsorption/sorption challenged with increasing concentrations of nonlabeled proteins. Lenses were soaked in phosphate-buffered saline to determine desorption. Results: Group IV lenses bound large amounts of lysozyme, whereas group I lenses bound highest amounts of albumin. Albumin binding to both lens types was relatively strong and could not be competed from binding by other proteins lysozyme, lactoferrin, and mucin. Mucin at high concentrations tended to positively cooperate with the binding of lactoferrin and albumin to all lenses. Conclusions: Binding of proteins to hydroxyethyl methacrylate-based hydrogel lens surfaces is affected by charge and polymer components, and perhaps manufacturing processes. Albumin binds strongly to lens surfaces, and this may play an adverse role during contact lens wear. © 2009 Lippincott Williams & Wilkins.	en_US
dc.relation.ispartof	Eye and Contact Lens	en_US
dc.relation.isbasedon	10.1097/ICL.0b013e3181becd3c	en_US
dc.subject.classification	Ophthalmology & Optometry	en_US
dc.subject.mesh	Humans	en_US
dc.subject.mesh	Methacrylates	en_US
dc.subject.mesh	Muramidase	en_US
dc.subject.mesh	Albumins	en_US
dc.subject.mesh	Lactoferrin	en_US
dc.subject.mesh	Eye Proteins	en_US
dc.subject.mesh	Mucins	en_US
dc.subject.mesh	Contact Lenses, Hydrophilic	en_US
dc.subject.mesh	Temperature	en_US
dc.subject.mesh	Binding, Competitive	en_US
dc.subject.mesh	Adsorption	en_US
dc.subject.mesh	Osmolar Concentration	en_US
dc.subject.mesh	Time Factors	en_US
dc.subject.mesh	In Vitro Techniques	en_US
dc.title	In vitro adsorption of tear proteins to hydroxyethyl methacrylate-based contact lens materials	en_US
dc.type	Journal Article
utslib.citation.volume	6	en_US
utslib.citation.volume	35	en_US
utslib.for	1113 Opthalmology and Optometry	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	6	en_US
pubs.publication-status	Published	en_US
pubs.volume	35	en_US

Abstract:

Objectives: Investigations of polymer interactions in single protein solutions is a necessary step in the elucidation of in vivo early binding events during protein deposition on hydroxyethyl methacrylate-based contact lens materials. Quantity and tenacity of binding of significant tear components to groups I and IV contact lenses was assessed. Competitive binding by these components was also examined. Methods: Adsorption on FDA groups I and IV hydrogel lenses was monitored using I-labeled protein. Lenses were incubated in increasing concentrations of radiolabeled single species proteins in solution. For competition experiments, concentration of each radiolabeled protein was held constant and the adsorption/sorption challenged with increasing concentrations of nonlabeled proteins. Lenses were soaked in phosphate-buffered saline to determine desorption. Results: Group IV lenses bound large amounts of lysozyme, whereas group I lenses bound highest amounts of albumin. Albumin binding to both lens types was relatively strong and could not be competed from binding by other proteins lysozyme, lactoferrin, and mucin. Mucin at high concentrations tended to positively cooperate with the binding of lactoferrin and albumin to all lenses. Conclusions: Binding of proteins to hydroxyethyl methacrylate-based hydrogel lens surfaces is affected by charge and polymer components, and perhaps manufacturing processes. Albumin binds strongly to lens surfaces, and this may play an adverse role during contact lens wear. © 2009 Lippincott Williams & Wilkins.

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