The DSpace digital repository system captures, stores, indexes, preserves, and distributes digital research material. http://dspace-roma3.caspur.it:80 2013-05-26T08:54:27Z 2013-05-26T08:54:27Z Dettin, Monica Thushari, Herat Gambaretto, Roberta Iucci, Giovanna Battocchio, Chiara Bagno, Andrea Ghezzo, Francesca Di Bello, Carlo Polzonetti, Giovanni Di Silvio, Lucy http://hdl.handle.net/2307/323 2011-12-22T13:35:28Z 2009-10-31T23:00:00Z

<Title>Assessment of novel chemical strategies for covalent attachment of adhesive peptides to rough titanium surfaces: XPS analysis and biological evaluation</Title> <Authors>Dettin, Monica; Thushari, Herat; Gambaretto, Roberta; Iucci, Giovanna; Battocchio, Chiara; Bagno, Andrea; Ghezzo, Francesca; Di Bello, Carlo; Polzonetti, Giovanni; Di Silvio, Lucy</Authors> <Issue Date>2009-11</Issue Date> <Is part of>Journal of Biomedical Materials Research A</Is part of> <Volume>91A</Volume> <Pages>463-479</Pages> <Abstract>Bioactive molecules have been proposed to promote beneficial interactions at bone-implant interfaces for enhancing integration. The main objective of this study was to develop novel methods to functionalize oxidized titanium surfaces by the covalent immobilization of bioactive peptides, through selective reaction involving single functional groups. In the first protocol, an aminoalkylsilane was covalently linked to the Ti oxide layer, followed by covalent binding of glutaric anhydride to the free NH2 groups. The carboxylic group Of glutaric anhydride was used to condense the free N-terminal group of the side-chain protected peptide sequence. Finally, the Surface was treated with trifluoroacetic acid to deprotect side-chain groups. In the second protocol, the peptide was directly anchored to the Ti oxide surface via UV activation of an arylazide peptide analogue. X-ray photoelectron spectroscopy analyses confirmed that modifications induced onto surface composition were in agreement with the reactions performed. The peptide density of each biomimetic Surface was determined on the basis of radiolabeling and XPS derived reaction yields. The in vitro cellular response of the biomimetic surfaces was evaluated using a primary human osteoblast cell model. Cell adhesion, proliferation, differentiation, and mineralization were examined at initial-, short-, and long-time periods. In was shown that the biomimetic surface obtained through photoprobe-marked analogue that combines an easily-performed modification provides a favorable surface for an enhanced cellular response. (C) 2008 Wiley Periodicals, Inc. J Biomed Mater Res 91A: 463-479, 200</Abstract>

2009-10-31T23:00:00Z Dettin, Monica Herath, Thushari Gambaretto, Roberta Iucci, Giovanna Battocchio, Chiara Bagno, Andrea Ghezzo, Francesca Di Bello, Carlo Polzonetti, Giovanni Di Silvio, Lucy http://hdl.handle.net/2307/256 2011-12-22T13:35:27Z 2009-10-31T23:00:00Z

<Title>Assessment of novel chemical strategies for covalent attachment ofadhesive peptides to rough titanium surfaces: XPS analysis andbiological evaluation</Title> <Authors>Dettin, Monica; Herath, Thushari; Gambaretto, Roberta; Iucci, Giovanna; Battocchio, Chiara; Bagno, Andrea; Ghezzo, Francesca; Di Bello, Carlo; Polzonetti, Giovanni; Di Silvio, Lucy</Authors> <Issue Date>2009-11</Issue Date> <Is part of>Journal of biomedical materials research</Is part of> <Volume>91A</Volume> <Pages>463-479</Pages> <Abstract>Bioactive molecules have been proposed to promote beneficialinteractions at bone-implant interfaces for enhancing integration. Themain objective of this study was to develop novel methods tofunctionalize oxidized titanium surfaces by the covalent immobilizationof bioactive peptides, through selective reaction involving singlefunctional groups. In the first protocol, an aminoalkylsilane wascovalently linked to the Ti oxide layer, followed by covalent bindingof glutaric anhydride to the free NH2 groups. The carboxylic group Ofglutaric anhydride was used to condense the free N-terminal group ofthe side-chain protected peptide sequence. Finally, the Surface wastreated with trifluoroacetic acid to deprotect side-chain groups. Inthe second protocol, the peptide was directly anchored to the Ti oxidesurface via UV activation of an arylazide peptide analogue. X-rayphotoelectron spectroscopy analyses confirmed that modificationsinduced onto surface composition were in agreement with the reactionsperformed. The peptide density of each biomimetic Surface wasdetermined on the basis of radiolabeling and XPS derived reactionyields. The in vitro cellular response of the biomimetic surfaces wasevaluated using a primary human osteoblast cell model. Cell adhesion,proliferation, differentiation, and mineralization were examined atinitial-, short-, and long-time periods. In was shown that thebiomimetic surface obtained through photoprobe-marked analogue thatcombines an easily-performed modification provides a favorable surfacefor an enhanced cellular response. (C) 2008 Wiley Periodicals, Inc. JBiomed Mater Res 91A: 463-479, 2009</Abstract>

2009-10-31T23:00:00Z