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dc.contributor.authorDelivopoulos, Evangelos
dc.contributor.authorOuberai, Myriam
dc.contributor.authorCoffey, Paul D
dc.contributor.authorSwann, Marcus J
dc.contributor.authorShakesheff, Kevin M
dc.contributor.authorWelland, Mark
dc.date.accessioned2015-02-18T14:00:49Z
dc.date.available2015-02-18T14:00:49Z
dc.date.issued2015-02-01
dc.identifier.citationColloids and Surfaces B: Biointerfaces Volume 126, 1 February 2015, Pages 169–177. DOI: 10.1016/j.colsurfb.2014.12.020
dc.identifier.issn0927-7765
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/246866
dc.description.abstractAmong the range of materials used in bioengineering, parylene-C has been used in combination with silicon oxide and in presence of the serum proteins, in cell patterning. However, the structural properties of adsorbed serum proteins on these substrates still remain elusive. In this study, we use an optical biosensing technique to decipher the properties of fibronectin (Fn) and serum albumin adsorbed on parylene-C and silicon oxide substrates. Our results show the formation of layers with distinct structural and adhesive properties. Thin, dense layers are formed on parylene-C, whereas thicker, more diffuse layers are formed on silicon oxide. These results suggest that Fn acquires a compact structure on parylene-C and a more extended structure on silicon oxide. Nonetheless, parylene-C and silicon oxide substrates coated with Fn host cell populations that exhibit focal adhesion complexes and good cell attachment. Albumin adopts a deformed structure on parylene-C and a globular structure on silicon oxide, and does not support significant cell attachment on either surface. Interestingly, the co-incubation of Fn and albumin at the ratio found in serum, results in the preferential adsorption of albumin on parylene-C and Fn on silicon oxide. This finding is supported by the exclusive formation of focal adhesion complexes in differentiated mouse embryonic stem cells (CGR8), cultured on Fn/albumin coated silicon oxide, but not on parylene-C. The detailed information provided in this study on the distinct properties of layers of serum proteins on substrates such as parylene-C and silicon oxide is highly significant in developing methods for cell patterning.
dc.description.sponsorshipThis research was supported by the European Research Council (ERC) under the European Community's Seventh Framework Programme (FP7/2007-2013)/ERC grant agreement 227845, the Biotechnology and Biological Sciences Research Council (BBSRC) Grant (BB/H003843/1) and the Technology Strategy Board (KTP008511) between Farfield, Biolin Scientific AB and Prof. Jian R. Lu at Manchester University (UK).
dc.languageEnglish
dc.language.isoen
dc.publisherElsevier BV
dc.rightsAttribution 2.0 UK: England & Wales
dc.rights.urihttp://creativecommons.org/licenses/by/2.0/uk/
dc.subjectParylene-C
dc.subjectSilicon oxide
dc.subjectSerum protein adsorption
dc.subjectFibronectin
dc.subjectCell adhesion
dc.subjectBiosensing technique
dc.titleSerum protein layers on parylene-C and silicon oxide: effect on cell adhesion.
dc.typeArticle
dc.description.versionThis is the final published version. It first appeared at http://www.sciencedirect.com/science/article/pii/S0927776514006961#.
prism.endingPage177
prism.publicationDate2014
prism.publicationNameColloids Surf B Biointerfaces
prism.startingPage169
prism.volume126
dc.rioxxterms.funderERC
dc.rioxxterms.funderEU FP7
dc.rioxxterms.funderBBSRC
dc.rioxxterms.projectidFP7/2007-2013
dc.rioxxterms.projectidBB/H003843/1
dcterms.dateAccepted2014-12-09
rioxxterms.versionofrecord10.1016/j.colsurfb.2014.12.020
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2014-12-16
dc.identifier.eissn1873-4367
rioxxterms.typeJournal Article/Review
pubs.funder-project-idBiotechnology and Biological Sciences Research Council (BB/H003843/1)


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Attribution 2.0 UK: England & Wales
Except where otherwise noted, this item's licence is described as Attribution 2.0 UK: England & Wales