Thin films of vitronectin transferred by MAPLE

Sima, F; Davidson, P; Pauthe, E; Gallet, O; Anselme, K; Mihailescu, IN

Thin films of vitronectin transferred by MAPLE

Sima, F Davidson, P Pauthe, E Gallet, O Anselme, K Mihailescu, IN

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Publication Type:: Journal Article
Citation:: Applied Physics A: Materials Science and Processing, 2011, 105 (3), pp. 611 - 617
Issue Date:: 2011-11-01

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Field	Value	Language
dc.contributor.author	Sima, F	en_US
dc.contributor.author	Davidson, P	en_US
dc.contributor.author	Pauthe, E	en_US
dc.contributor.author	Gallet, O	en_US
dc.contributor.author	Anselme, K	en_US
dc.contributor.author	Mihailescu, IN	en_US
dc.date.accessioned	2017-09-25T04:34:45Z
dc.date.available	2017-09-25T04:34:45Z
dc.date.issued	2011-11-01	en_US
dc.identifier.citation	Applied Physics A: Materials Science and Processing, 2011, 105 (3), pp. 611 - 617	en_US
dc.identifier.issn	0947-8396	en_US
dc.identifier.uri	http://hdl.handle.net/10453/117667
dc.description.abstract	We report on matrix-assisted pulsed laser evaporation (MAPLE) transfer of intact and functional protein molecules from a cryogenic aliquot obtained by freezing a protein-saline buffer solution. Vitronectin (Vn), an extracellular matrix protein with distinctive active domains for cell attachment and signalization, was expelled from frozen targets by KrF*excimer laser irradiation, and then immobilized on substrates. Particulates surrounded by a dense matrix were observed by optical, profilometry and AFM studies. The composition preservation of MAPLE-deposited protein films versus drop-cast films was demonstrated by FTIR and immunostaining studies. The stability and integrity of Vn after transfer was shown by their interaction with human osteoprogenitor cells in which actin filaments stretched across the entire cell area and clear focal points with surface were formed. The absence of detectable degradation of protein structure after MAPLE immobilization could provide benefits to surface functionalization for biomedical applications. © 2011 Springer-Verlag.	en_US
dc.relation.ispartof	Applied Physics A: Materials Science and Processing	en_US
dc.relation.isbasedon	10.1007/s00339-011-6601-z	en_US
dc.subject.classification	Applied Physics	en_US
dc.title	Thin films of vitronectin transferred by MAPLE	en_US
dc.type	Journal Article
utslib.citation.volume	3	en_US
utslib.citation.volume	105	en_US
utslib.for	0204 Condensed Matter Physics	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 Health
pubs.organisational-group	/University of Technology Sydney/Strength - AAI - Advanced Analytics Research Centre
pubs.organisational-group	/University of Technology Sydney/Strength - CHSP - Health Services and Practice
utslib.copyright.status	closed_access
pubs.declined	2017-09-25T14:34:45.354+1000
pubs.deleted	2017-09-25T14:34:45.354+1000
pubs.issue	3	en_US
pubs.publication-status	Published	en_US
pubs.volume	105	en_US

Abstract:

We report on matrix-assisted pulsed laser evaporation (MAPLE) transfer of intact and functional protein molecules from a cryogenic aliquot obtained by freezing a protein-saline buffer solution. Vitronectin (Vn), an extracellular matrix protein with distinctive active domains for cell attachment and signalization, was expelled from frozen targets by KrF*excimer laser irradiation, and then immobilized on substrates. Particulates surrounded by a dense matrix were observed by optical, profilometry and AFM studies. The composition preservation of MAPLE-deposited protein films versus drop-cast films was demonstrated by FTIR and immunostaining studies. The stability and integrity of Vn after transfer was shown by their interaction with human osteoprogenitor cells in which actin filaments stretched across the entire cell area and clear focal points with surface were formed. The absence of detectable degradation of protein structure after MAPLE immobilization could provide benefits to surface functionalization for biomedical applications. © 2011 Springer-Verlag.

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http://hdl.handle.net/10453/117667