Protein adsorption on derivatives of hyaluronan

Lord, MS; Pasqui, D; Barbucci, R; Milthorpe, BK

Protein adsorption on derivatives of hyaluronan

Lord, MS Pasqui, D Barbucci, R Milthorpe, BK

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Publication Type:: Journal Article
Citation:: Macromolecular Symposia, 2008, 266 (1), pp. 17 - 22
Issue Date:: 2008-06-01

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Field	Value	Language
dc.contributor.author	Lord, MS	en_US
dc.contributor.author	Pasqui, D	en_US
dc.contributor.author	Barbucci, R	en_US
dc.contributor.author	Milthorpe, BK https://orcid.org/0000-0002-0867-9586	en_US
dc.date.issued	2008-06-01	en_US
dc.identifier.citation	Macromolecular Symposia, 2008, 266 (1), pp. 17 - 22	en_US
dc.identifier.issn	1022-1360	en_US
dc.identifier.uri	http://hdl.handle.net/10453/8453
dc.description.abstract	Serum protein adsorption and fibroblast cell adhesion on photo reactive hyaluronic acid (Hyal-N3) and its sulfated derivative (HyalS-N 3) was analysed using a combination of quartz crystal microbalance (QCM) and cell adhesion assays. There was no significant differences in the amount of protein adsorbed onto the two polymers, however proteins were found to be more loosely bound to HyalS-N3 compared with Hyal-N3. Approximately 17% and 31% of the fibronectin interacting with Hyal-N3 and HyalS-N3 respectively was found to be irreversibly bound after rinsing with MilliQ water, SDS and urea. Proteins were exposed to the polymers before cell adhesion was monitored for a period of 2 hours in serum free conditions. Minimal cell adhesion was observed on albumin-coated materials as well as serum precoated Hyal-N3. Precoating the materials with fibronectin enhanced cell adhesion, although HyalS-N3 experienced higher levels of cell adhesion than Hyal-N3 and similar results were found for the serum precoated materials. Copyright © 2008 WILEY-VCH Verlag GmbH & Co. KGaA.	en_US
dc.relation.ispartof	Macromolecular Symposia	en_US
dc.relation.isbasedon	10.1002/masy.200850604	en_US
dc.title	Protein adsorption on derivatives of hyaluronan	en_US
dc.type	Journal Article
utslib.citation.volume	1	en_US
utslib.citation.volume	266	en_US
utslib.for	0303 Macromolecular and Materials Chemistry	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	1	en_US
pubs.publication-status	Published	en_US
pubs.volume	266	en_US

Abstract:

Serum protein adsorption and fibroblast cell adhesion on photo reactive hyaluronic acid (Hyal-N3) and its sulfated derivative (HyalS-N 3) was analysed using a combination of quartz crystal microbalance (QCM) and cell adhesion assays. There was no significant differences in the amount of protein adsorbed onto the two polymers, however proteins were found to be more loosely bound to HyalS-N3 compared with Hyal-N3. Approximately 17% and 31% of the fibronectin interacting with Hyal-N3 and HyalS-N3 respectively was found to be irreversibly bound after rinsing with MilliQ water, SDS and urea. Proteins were exposed to the polymers before cell adhesion was monitored for a period of 2 hours in serum free conditions. Minimal cell adhesion was observed on albumin-coated materials as well as serum precoated Hyal-N3. Precoating the materials with fibronectin enhanced cell adhesion, although HyalS-N3 experienced higher levels of cell adhesion than Hyal-N3 and similar results were found for the serum precoated materials. Copyright © 2008 WILEY-VCH Verlag GmbH & Co. KGaA.

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http://hdl.handle.net/10453/8453