Please use this identifier to cite or link to this item: https://apo.ansto.gov.au/dspace/handle/10238/8689
Title: Assessment of a fast generated analytical matrix for rotating slat collimation iterative reconstruction: a possible method to optimize the collimation profile
Authors: Boisson, F
Bekaert, V
Reilhac, A
Wurtz, J
Brasse, D
Keywords: Visible radiation
Polystyrene
Data
Biological models
Nuutron reflections
Carbon sources
Issue Date: 26-Feb-2015
Publisher: IOP Science
Citation: Boisson, F., Bekaert, V., Reilhac, A., Wurtz, J., & Brasse, D. (2015). Assessment of a fast generated analytical matrix for rotating slat collimation iterative reconstruction: a possible method to optimize the collimation profile. Physics in Medicine and Biology, 60(6), 2403-2419. doi:10.1088/0031-9155/60/6/2403
Abstract: A polystyrene film spun onto polished silicon substrates was implanted with argon ions using plasma immersion ion implantation (PIII) to activate its surface for single-step immobilization of biological molecules. The film was subsequently investigated by X-ray and neutron reflectometry, ultraviolet (UV)–visible (vis) and Fourier transform infrared (FTIR) ellipsometry, FTIR and Raman spectroscopy, as well as nuclear reaction analysis to determine the structural and compositional transformations associated with the surface activation. The ion irradiation resulted in a significant densification of the carbon structure, which was accompanied by hydrogen loss. The density and hydrogen profiles in the modified surface layers were found to agree with the expected depths of ion implantation as calculated by the Stopping and Range of Ions in Matter (SRIM) software. The data demonstrate that the reduction in film thickness is due to ion-induced densification rather than the removal of material by etching. Characterization by FTIR, atomic force microscopy (AFM), ellipsometry, and X-ray reflectometry shows that polystyrene films modified in this way immobilize dense layers of protein (tropoelastin) directly from solution. A substantial fraction of the immobilized protein layer remains after rigorous washing with sodium dodecyl sulfate solution, indicating that its immobilization is by covalent bonding. © Copyright 2020 IOP Publishing
Gov't Doc #: 8185
URI: http://dx.doi.org/10.1088/0031-9155/60/6/2403
http://apo.ansto.gov.au/dspace/handle/10238/8689
Appears in Collections:Journal Articles

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