Human serum albumin adsorption on hydrogel contact lenses in vitro

Garrett, Q; Milthorpe, BK

Human serum albumin adsorption on hydrogel contact lenses in vitro

Garrett, Q Milthorpe, BK

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Publication Type:: Journal Article
Citation:: Investigative Ophthalmology and Visual Science, 1996, 37 (13), pp. 2594 - 2602
Issue Date:: 1996-12-01

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Field	Value	Language
dc.contributor.author	Garrett, Q	en_US
dc.contributor.author	Milthorpe, BK https://orcid.org/0000-0002-0867-9586	en_US
dc.date.issued	1996-12-01	en_US
dc.identifier.citation	Investigative Ophthalmology and Visual Science, 1996, 37 (13), pp. 2594 - 2602	en_US
dc.identifier.issn	0146-0404	en_US
dc.identifier.uri	http://hdl.handle.net/10453/9779
dc.description.abstract	Purpose. To improve the understanding of the formation of protein deposits on hydrogel lenses. Methods. A study of protein adsorption on three commercial hydrogel contact lenses of different materials. Etafilcon A (2- hydroxyethyl methacrylate [HEMA] polymer with sodium methacrylate and 2- ethyl-2-hydroxymethyl-1,3-propanediol trimethacrylate), tefilcon (poly[HEMA] cross-linked and copolymerized with ethylene glycol dimethacrylate), and vifilcon A (methacrylic acid polymer with ethylene glycol dimethacrylate, HEMA and N-vinyl pyrrolidone) was undertaken by using a single protein solution, human serum albumin (HSA), and a radiolabel-tracer technique. Results. Static adsorption leading to multilayer adsorption was observed. Complete reversibility for adsorbed HSA on lenses did not exist. Some was tightly bound, whereas most was loosely bound and could be removed easily by rinsing in phosphate-buffered saline. Irreversible adsorption of HSA on the lenses was found to be time dependent and did not reach a maximum value even after 48 hours of adsorption. The amount of HSA adsorbed on the lenses- irreversibly as well as totally adsorbed protein-was in the order of vifilcon A > tefilcon > etafilcon A. Adsorption of HSA on the lenses increases with decreasing pH (range, 7.4 to 4) but always follows the above trend with respect to the different types of lenses. Conclusions. Irreversible binding of HSA on lenses is governed by the kinetics of protein denaturation. Electrostatic interactions may not play a major role in HSA adsorption on hydrogel lenses. Some other factors, such as hydrophobic dehydration, and special monomer units, such as N-vinyl pyrrolidone in the lens materials, may favor adsorption of HSA.	en_US
dc.relation.ispartof	Investigative Ophthalmology and Visual Science	en_US
dc.subject.classification	Ophthalmology & Optometry	en_US
dc.subject.mesh	Humans	en_US
dc.subject.mesh	Polyethylene Glycols	en_US
dc.subject.mesh	Hydrogel	en_US
dc.subject.mesh	Serum Albumin	en_US
dc.subject.mesh	Contact Lenses	en_US
dc.subject.mesh	Protein Binding	en_US
dc.subject.mesh	Protein Denaturation	en_US
dc.subject.mesh	Kinetics	en_US
dc.subject.mesh	Adsorption	en_US
dc.subject.mesh	Hydrogen-Ion Concentration	en_US
dc.subject.mesh	Hydrogel, Polyethylene Glycol Dimethacrylate	en_US
dc.title	Human serum albumin adsorption on hydrogel contact lenses in vitro	en_US
dc.type	Journal Article
utslib.citation.volume	13	en_US
utslib.citation.volume	37	en_US
utslib.for	110106 Medical Biochemistry: Proteins and Peptides (incl. Medical Proteomics)	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	13	en_US
pubs.publication-status	Published	en_US
pubs.volume	37	en_US

Abstract:

Purpose. To improve the understanding of the formation of protein deposits on hydrogel lenses. Methods. A study of protein adsorption on three commercial hydrogel contact lenses of different materials. Etafilcon A (2- hydroxyethyl methacrylate [HEMA] polymer with sodium methacrylate and 2- ethyl-2-hydroxymethyl-1,3-propanediol trimethacrylate), tefilcon (poly[HEMA] cross-linked and copolymerized with ethylene glycol dimethacrylate), and vifilcon A (methacrylic acid polymer with ethylene glycol dimethacrylate, HEMA and N-vinyl pyrrolidone) was undertaken by using a single protein solution, human serum albumin (HSA), and a radiolabel-tracer technique. Results. Static adsorption leading to multilayer adsorption was observed. Complete reversibility for adsorbed HSA on lenses did not exist. Some was tightly bound, whereas most was loosely bound and could be removed easily by rinsing in phosphate-buffered saline. Irreversible adsorption of HSA on the lenses was found to be time dependent and did not reach a maximum value even after 48 hours of adsorption. The amount of HSA adsorbed on the lenses- irreversibly as well as totally adsorbed protein-was in the order of vifilcon A > tefilcon > etafilcon A. Adsorption of HSA on the lenses increases with decreasing pH (range, 7.4 to 4) but always follows the above trend with respect to the different types of lenses. Conclusions. Irreversible binding of HSA on lenses is governed by the kinetics of protein denaturation. Electrostatic interactions may not play a major role in HSA adsorption on hydrogel lenses. Some other factors, such as hydrophobic dehydration, and special monomer units, such as N-vinyl pyrrolidone in the lens materials, may favor adsorption of HSA.

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