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231223s2009 xx |||||o 00| ||eng c |
| 024 |
7 |
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|a 10.1021/la8028275
|2 doi
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|a pubmed24n0622.xml
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|a (DE-627)NLM186535376
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|a (NLM)19227984
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Syahir, Amir
|e verfasserin
|4 aut
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| 245 |
1 |
0 |
|a Poly(amidoamine)-dendrimer-modified gold surfaces for anomalous reflection of gold to detect biomolecular interactions
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| 264 |
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1 |
|c 2009
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| 336 |
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 15.09.2009
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|a Date Revised 21.11.2013
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|a published: Print
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|a Citation Status MEDLINE
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|a 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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4 |
|a Journal Article
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| 650 |
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4 |
|a Research Support, Non-U.S. Gov't
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| 650 |
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7 |
|a Amides
|2 NLM
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| 650 |
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7 |
|a Amines
|2 NLM
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| 650 |
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7 |
|a Dendrimers
|2 NLM
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| 650 |
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7 |
|a Immunoglobulin G
|2 NLM
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| 650 |
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7 |
|a Proteins
|2 NLM
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| 650 |
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7 |
|a Avidin
|2 NLM
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| 650 |
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7 |
|a 1405-69-2
|2 NLM
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| 650 |
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7 |
|a Biotin
|2 NLM
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| 650 |
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7 |
|a 6SO6U10H04
|2 NLM
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| 650 |
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7 |
|a Gold
|2 NLM
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| 650 |
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7 |
|a 7440-57-5
|2 NLM
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| 700 |
1 |
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|a Tomizaki, Kin-Ya
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Kajikawa, Kotaro
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Mihara, Hisakazu
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 25(2009), 6 vom: 09. Apr., Seite 3667-74
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
1 |
8 |
|g volume:25
|g year:2009
|g number:6
|g day:09
|g month:04
|g pages:3667-74
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| 856 |
4 |
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|u http://dx.doi.org/10.1021/la8028275
|3 Volltext
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|d 25
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|h 3667-74
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