Protein interaction with combinatorial structures

Luisa Filipponi; Elena P. Ivanova; Andrea Viezzoli; Dan V. Nicolau

doi:10.1117/12.469737

14 November 2002 Protein interaction with combinatorial structures

Luisa Filipponi, Elena P. Ivanova, Andrea Viezzoli, Dan V. Nicolau

Proceedings Volume 4937, Biomedical Applications of Micro- and Nanoengineering; (2002) https://doi.org/10.1117/12.469737
Event: SPIE's International Symposium on Smart Materials, Nano-, and Micro- Smart Systems, 2002, Melbourne, Australia

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.

Citation Download Citation

Luisa Filipponi, Elena P. Ivanova, Andrea Viezzoli, and Dan V. Nicolau "Protein interaction with combinatorial structures", Proc. SPIE 4937, Biomedical Applications of Micro- and Nanoengineering, (14 November 2002); https://doi.org/10.1117/12.469737

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