Linked Life Data

18261887

Source:http://linkedlifedata.com/resource/pubmed/id/18261887

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-5-5
pubmed:abstractText
The 9th-10th type III fibronectin domain pair (9-10FNIII) has found widespread use as a biomimetic surface for cell adhesion. However, the effect of mutations to 9-10FNIII on its surface adsorption characteristics have not been investigated. Here we address this issue using total internal reflection fluorescence (TIRF) and circular dichroism spectroscopy, comparing two conformationally stable 9-10FNIII mutants against the wild type. Desorption of the 9-10FNIII mutants from the silica surface was minimal in comparison to desorption of 9-10FNIII. The extent and rate of protein desorption from silica was empirically matched by loss of secondary structure upon adsorption, with only the spectrum for 9-10FNIII showing extensive loss of the beta-sandwich fold. For the proteins adsorbed to hydrophobic surfaces, only the CD spectra for the 9-10FNIII mutant constrained via an interdomain disulphide bridge showed similarity with the corresponding solution structure. Since the binding of 9-10FNIII to integrin alpha5beta1 is highly dependent on the relative spatial arrangement of the two domains, we suggest that the observed differences in cell adhesion and spreading on wild type 9-10FNIII and mutants may in part be attributed to the extent of protein desorption and unfolding at the surface.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0927-7765
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
64
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-9
pubmed:dateRevised
2009-10-16
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Interdomain mobility and conformational stability of type III fibronectin domain pairs control surface adsorption, desorption and unfolding.
pubmed:affiliation
Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, 27 Taylor Street, Glasgow, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't