Poly(amidoamine)-dendrimer-modified gold surfaces for anomalous reflection of gold to detect biomolecular interactions
Label-free protein detecting chip technology has encouraged a number of discoveries, as it is a powerful analytical tool in the postgenomic era. In particular, we have focused on a unique characteristic of anomalous reflection of gold (AR) as a new class of label-free detection method for a protein...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 25(2009), 6 vom: 09. Apr., Seite 3667-74 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2009
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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 Amides Amines Dendrimers Immunoglobulin G Proteins Avidin 1405-69-2 Biotin mehr... |
| Zusammenfassung: | Label-free protein detecting chip technology has encouraged a number of discoveries, as it is a powerful analytical tool in the postgenomic era. In particular, we have focused on a unique characteristic of anomalous reflection of gold (AR) as a new class of label-free detection method for a protein chip system. In this paper, in order to improve the sensitivity of detection of biomolecular interactions by the AR method, we have constructed three-dimensional (3D) nanostructures on gold surfaces with a series of well-defined structures of poly(amidoamine) dendrimers (PAMAMs) from generation 2 to 4 (G2, G3, and G4) tethering biotin moieties as capturing agents for avidin and antibiotin IgG. Comparison of features of such 3D nanostructured surfaces with a diamine-modified flat-like surface revealed a 2-fold increase in the amount of avidin for 3D surfaces relative to the flat surface, and surface-assisted nonspecific interactions were significantly suppressed. We thus obtained 91% coverage for avidin detection on the PAMAM G4-modified surface, indicating a theoretically maximum attainable absorption considering a hexagonal-packed arrangement as a saturated monomolecular layer. In the antibiotin IgG assay, the PAMAM G4-modified surface clearly improved the amount of proteins captured compared to that for the flat surface, indicating that an appropriate density of capturing agents played a more important role in the interaction of larger molecular-sized proteins such as antibiotin IgG, which requires more space for interaction than the medium-sized avidin. These findings should assist in the development of a simple and practical tool for high-throughput protein detection, particularly with the AR method |
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| Beschreibung: | Date Completed 15.09.2009 Date Revised 21.11.2013 published: Print Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la8028275 |