Electrochemical analysis of azurin thermodynamic and adsorption properties at monolayer-protected cluster film assemblies - evidence for a more homogeneous adsorption interface
| Autor: | Tran T. Doan, Jonathan D. Dattelbaum, Christopher P. Gulka, Matthew L. Trawick, Morgan Lynn Vargo, John K. Gerig, Michael C. Leopold |
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| Rok vydání: | 2010 |
| Předmět: |
education.field_of_study
Chemistry Population Analytical chemistry Nanoparticle Self-assembled monolayer Membranes Artificial Surfaces Coatings and Films Electronic Optical and Magnetic Materials Biomaterials Kinetics Colloid and Surface Chemistry Adsorption Chemical engineering Azurin Desorption Monolayer Pseudomonas aeruginosa Electrochemistry Thermodynamics education Electrodes Protein adsorption |
| Zdroj: | Journal of colloid and interface science. 352(1) |
| ISSN: | 1095-7103 |
| Popis: | Thermodynamic and adsorption properties of protein monolayer electrochemistry (PME) are examined for Pseudomonas aeruginosa azurin (AZ) immobilized at an electrode modified with a networked film of monolayer-protected clusters (MPCs) to assess if nanoparticle films of this nature offer a more homogeneous adsorption interface compared to traditional self-assembled monolayer (SAM) modified electrodes. Specifically, electrochemistry is used to assess properties of surface coverage, formal potential, peak broadening, and electron transfer (ET) kinetics as a function of film thickness. The modification of a surface with dithiol-linked films of MPCs (Au(225)C6(75)) provides a more uniform binding interface for AZ that results in voltammetry with less peak broadening (110mV) compared to SAMs (120-130mV). Improved homogeneity of the MPC interface for protein adsorption is confirmed by atomic force microscopy imaging that shows uniform coverage of the gold substrate topography and by electrochemical analysis of film properties during systematic desorption of AZ, which indicates a more homogeneous population of adsorbed protein at MPC films. These results suggest MPC film assemblies may be used in PME to provide greater molecular level control of the protein adsorption interface, a development with applications for strategies to study biological ET processes as well as the advancement of biosensor technologies. |
| Databáze: | OpenAIRE |
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