Irreversible adsorption of human serum albumin to hydrogel contact lenses: A study using electron spin resonance spectroscopy

Garrett, Q; Griesser, HJ; Milthorpe, BK; Garrett, RW

Irreversible adsorption of human serum albumin to hydrogel contact lenses: A study using electron spin resonance spectroscopy

Garrett, Q Griesser, HJ Milthorpe, BK

Garrett, RW

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Publication Type:: Journal Article
Citation:: Biomaterials, 1999, 20 (14), pp. 1345 - 1356
Issue Date:: 1999-07-01

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Field	Value	Language
dc.contributor.author	Garrett, Q	en_US
dc.contributor.author	Griesser, HJ	en_US
dc.contributor.author	Milthorpe, BK https://orcid.org/0000-0002-0867-9586	en_US
dc.contributor.author	Garrett, RW	en_US
dc.date.issued	1999-07-01	en_US
dc.identifier.citation	Biomaterials, 1999, 20 (14), pp. 1345 - 1356	en_US
dc.identifier.issn	0142-9612	en_US
dc.identifier.uri	http://hdl.handle.net/10453/9682
dc.description.abstract	Human serum albumin (HSA) was specifically spin labelled with 4-maleimido-tempo (MSL) at its cysteine 34 residue (HSA-MSL). The irreversible adsorption of HSA-MSL to hydrogel contact lenses (etafilcon A, tefilcon and vifilcon A) was investigated using electron spin resonance (ESR) spectroscopy. Changes in ESR spectral characteristics of adsorbed HSA-MSL as compared to HSA-MSL in solution displayed an additional immobilisation of the spin label due to the adsorption. This immobilisation of MSL corresponds to a large conformational alteration of the HSA-MSL near the modified Cys 34 residue. For both etafilcon A and tefilcon, the rate of irreversible adsorption was relatively slow compared with that of vifilcon A where the maximum state of immobilisation and hence conformational change occurred within the first hour of adsorption. Furthermore, tefilcon produced markedly different ESR spectra where a strong conformational change to a less mobile protein was apparent. This supported a model where the direct irreversible adsorption of HSA from solution dominated on tefilcon as opposed to conversion of the adsorbed protein from the reversible to the irreversible state on both etafilcon A and vifilcon A. HSA-MSL adsorption onto hydrophobic poly(methylmethacrylate) (PMMA) and hydrophilic poly(N-ter-butylacrylamide) (PTBAM) latex beads was also investigated. The spin label MSL was found to be less mobile when HSA was adsorbed onto PMMA compared with PTBAM beads. It was also found that the rate of irreversible adsorption of HSA is far higher onto PMMA surfaces than onto PTBAM surfaces.	en_US
dc.relation.ispartof	Biomaterials	en_US
dc.relation.isbasedon	10.1016/S0142-9612(99)00037-X	en_US
dc.subject.classification	Biomedical Engineering	en_US
dc.subject.mesh	Humans	en_US
dc.subject.mesh	Spin Labels	en_US
dc.subject.mesh	Cysteine	en_US
dc.subject.mesh	Cyclic N-Oxides	en_US
dc.subject.mesh	Serum Albumin	en_US
dc.subject.mesh	Hydrogels	en_US
dc.subject.mesh	Electron Spin Resonance Spectroscopy	en_US
dc.subject.mesh	Contact Lenses, Hydrophilic	en_US
dc.subject.mesh	Protein Conformation	en_US
dc.subject.mesh	Kinetics	en_US
dc.subject.mesh	Adsorption	en_US
dc.subject.mesh	Time Factors	en_US
dc.title	Irreversible adsorption of human serum albumin to hydrogel contact lenses: A study using electron spin resonance spectroscopy	en_US
dc.type	Journal Article
utslib.citation.volume	14	en_US
utslib.citation.volume	20	en_US
utslib.for	090302 Biomechanical Engineering	en_US
utslib.for	090301 Biomaterials	en_US
utslib.for	110304 Dermatology	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	14	en_US
pubs.publication-status	Published	en_US
pubs.volume	20	en_US

Abstract:

Human serum albumin (HSA) was specifically spin labelled with 4-maleimido-tempo (MSL) at its cysteine 34 residue (HSA-MSL). The irreversible adsorption of HSA-MSL to hydrogel contact lenses (etafilcon A, tefilcon and vifilcon A) was investigated using electron spin resonance (ESR) spectroscopy. Changes in ESR spectral characteristics of adsorbed HSA-MSL as compared to HSA-MSL in solution displayed an additional immobilisation of the spin label due to the adsorption. This immobilisation of MSL corresponds to a large conformational alteration of the HSA-MSL near the modified Cys 34 residue. For both etafilcon A and tefilcon, the rate of irreversible adsorption was relatively slow compared with that of vifilcon A where the maximum state of immobilisation and hence conformational change occurred within the first hour of adsorption. Furthermore, tefilcon produced markedly different ESR spectra where a strong conformational change to a less mobile protein was apparent. This supported a model where the direct irreversible adsorption of HSA from solution dominated on tefilcon as opposed to conversion of the adsorbed protein from the reversible to the irreversible state on both etafilcon A and vifilcon A. HSA-MSL adsorption onto hydrophobic poly(methylmethacrylate) (PMMA) and hydrophilic poly(N-ter-butylacrylamide) (PTBAM) latex beads was also investigated. The spin label MSL was found to be less mobile when HSA was adsorbed onto PMMA compared with PTBAM beads. It was also found that the rate of irreversible adsorption of HSA is far higher onto PMMA surfaces than onto PTBAM surfaces.

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http://hdl.handle.net/10453/9682