Linked Life Data

20170253

Source:http://linkedlifedata.com/resource/pubmed/id/20170253

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-2-22
pubmed:abstractText
Bovine serum albumin (BSA) protein adsorption on thin spun films of different metal octakishexylthiophthalocyanine [(C(6)S)(8)PcM, M=Cu, Ni] derivatives is investigated by using three independent spectroscopic measurements namely Raman spectroscopy, ellipsometry and surface plasmon resonance imaging. Thermally induced molecular self-reorganisations in the phthalocyanine films are found to have produced the changes in the surface energy which, in turn, control protein adsorption. The amount of BSA adsorption on [(C(6)S)(8)PcNi] is more limited than that on [(C(6)S)(8)PcCu] and this observation is consistent with the results on the surface wettability obtained from the contact angle measurements. The shift from the plasmonic resonance wavelength because of the BSA adsorption was significantly larger for the heat-treated [(C(6)S)(8)PcCu] than as-deposited film. Similar measurements on the [(C(6)S)(8)PcNi] films showed a limited BSA adsorption. The results of surface plasmon resonance experiments are consistent with those obtained from Raman spectroscopic and ellipsometric techniques.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1751-8741
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-9
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Characterisation of protein adsorption on different liquid crystal phthalocyaninethin films.
pubmed:affiliation
Queen Mary, University of London, School of Engineering and Material Science, London, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't