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

Adsorption

Photoresist materials

Polymers

Biosensors

Absorption

Molecules

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