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Proceedings Paper

Protein interaction with combinatorial structures
Author(s): Luisa Filipponi; Elena P. Ivanova; Andrea Viezzoli; Dan V. Nicolau
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Paper Abstract

Diazonaphthoquinone/novolak (DNQ) photoresist have the property of changing physical-chemical properties during exposure to UV light, which reflects in a change of the polymer hydrophobicity. A combinatorial surface having different exposed area was fabricated, in order to study the influence of hydrophobicity over protein adsorption and EDC-mediated covalent attachment. The results indicate two different behaviours, reflecting a substantial different mechanism of interaction. While protein adsorption decreased following the hydrophobicity decrease, covalent attachment increased, thus reflecting the effectiveness of the covalent mediator, which cross-links the protein to the carboxylic groups that form during exposure. Based on the results of the present work, a combinatorial microarray will be fabricated, to be used in the biosensor field.

Paper Details

Date Published: 14 November 2002
PDF: 6 pages
Proc. SPIE 4937, Biomedical Applications of Micro- and Nanoengineering, (14 November 2002); doi: 10.1117/12.469737
Show Author Affiliations
Luisa Filipponi, Swinburne Univ. of Technology (Australia)
Elena P. Ivanova, Swinburne Univ. of Technology (Australia)
Andrea Viezzoli, Swinburne Univ. of Technology (Australia)
Dan V. Nicolau, Swinburne Univ. of Technology (Australia)

Published in SPIE Proceedings Vol. 4937:
Biomedical Applications of Micro- and Nanoengineering
Dan V. Nicolau, Editor(s)

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