Modulating surface density of proteins via caged surfaces and controlled light exposure

We demonstrate the possibility of tuning the degree of functionalization of a surface using photoactivatable chemistries and controlled light exposure. A photosensitive organosilane with a protected amine terminal group and a tetraethyleneglycol spacer was synthesized. A o-nitrobenzyl cage was used...

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Bibliographische Detailangaben
Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 27(2011), 6 vom: 15. März, Seite 2789-95
1. Verfasser: Álvarez, Marta (VerfasserIn)
Weitere Verfasser: Alonso, José María, Filevich, Oscar, Bhagawati, Maniraj, Etchenique, Roberto, Piehler, Jacob, del Campo, Aránzazu
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2011
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Photosensitizing Agents Proteins
Beschreibung
Zusammenfassung:We demonstrate the possibility of tuning the degree of functionalization of a surface using photoactivatable chemistries and controlled light exposure. A photosensitive organosilane with a protected amine terminal group and a tetraethyleneglycol spacer was synthesized. A o-nitrobenzyl cage was used as the photoremovable group to cage the amine functionality. Surfaces with phototunable amine densities were generated by controlled irradiation of silica substrates modified with the photosensitive anchor. Protein layers with different densities could be obtained by successive coupling and assembly steps. Protein surface concentrations were quantified by reflectance interference. Our results demonstrate that the protein density correlates with the photogenerated ligand density. The density control was proved over four coupling steps (biotin, SAv, (BT)tris-NTA, MBP, or GFP), indicating that the interactions between underlying layer and soluble targets are highly specific and the immobilized targets at the four levels maintain their full functionality. Protein micropatterns with a gradient of protein density were also obtained
Beschreibung:Date Completed 21.10.2014
Date Revised 04.02.2014
published: Print-Electronic
Citation Status MEDLINE
ISSN:1520-5827
DOI:10.1021/la104511x