Engineering the interface between glucose oxidase and nanoparticles
The behavior of glucose oxidase (GOx) on gold nanoparticles (NPs) was investigated as a function of (1) NP surface chemistry, (2) stabilizing protein additives, and (3) protein microenvironment. GOx secondary structure and unfolding was probed by circular dichroism (CD) spectroscopy and fluorescence...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 28(2012), 11 vom: 20. März, Seite 5190-200 |
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| Weitere Verfasser: | , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2012
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Glucose Oxidase EC 1.1.3.4 |
| Zusammenfassung: | The behavior of glucose oxidase (GOx) on gold nanoparticles (NPs) was investigated as a function of (1) NP surface chemistry, (2) stabilizing protein additives, and (3) protein microenvironment. GOx secondary structure and unfolding was probed by circular dichroism (CD) spectroscopy and fluorescence, and GOx enzymatic activity was measured by a colorimetric assay. We also examined the activity and structure of GOx after displacement from the NP surface. Generally, GOx behavior was negatively impacted by conjugation to the NP, and conjugation conditions could vary the influence of the NP. Surface chemistry and protein microenvironment could improve behavior, but addition of stabilizing proteins negatively influenced activity. After displacement from the NPs, GOx tended to remain unfolded, indicating that the interactions with the NP were irreversible |
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| Beschreibung: | Date Completed 05.07.2012 Date Revised 20.03.2012 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la2050866 |