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231223s2007 xx ||||| 00| ||eng c |
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|a pubmed24n0582.xml
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|a (DE-627)NLM174508727
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|a (NLM)17949123
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Onodera, Kota
|e verfasserin
|4 aut
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|a Label-free detection of protein-protein interactions at the GaAs/water interface through surface infrared spectroscopy
|b discrimination between specific and nonspecific interactions by using secondary structure analysis
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|c 2007
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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|a Band
|b nc
|2 rdacarrier
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|a Date Completed 08.02.2008
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|a Date Revised 24.11.2016
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Here, we propose a label-free detection of protein-protein interactions that enables simultaneous qualitative analysis of target proteins by using Fourier transform infrared (FTIR) absorption spectroscopy in multiple internal reflection geometry (MIR-FTIR). Using this method, the target proteins were detected based on the peak height of the amide I and amide II bands, while discrimination of specific and nonspecific signals is made based on the secondary structure of the analytes, which is determined through second-derivative analysis of the amide I band. As a model system, an antigen peptide was immobilized on the surface of GaAs, which was transparent to mid-infrared light, and the interaction with its antibody was examined in aqueous media. We demonstrated that the binding of the antibody to the antigen immobilized on a GaAs surface selectively gave rise to beta-sheet amide I vibrations (1639 and 1690 cm-1), while no structurally related signals were induced by nonspecifically adsorbed proteins. The peak height of the beta-peak (1639 cm-1) in the amide I band linearly increased with the antiserum concentration as well as that of the amide II band. The detection limit (S/N = 3) was a 1:36 000 dilution for the amide I signal. In addition, through the use of surface-sensitive MIR-FTIR, the present sensor selectively detected the antigen-antibody interactions at the surfaces without being affected by the presence of bulk species, enabling rapid and wash-free detection. Our method provides not only rapid label-free detection of protein-protein interactions but a more accurate discrimination between specific and nonspecific interactions through the use of the secondary structure of the target proteins as a measure for the specific signals
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Arsenicals
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|a Peptides
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|a Proteins
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|a Water
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|a gallium arsenide
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|a Gallium
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|a CH46OC8YV4
|2 NLM
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| 700 |
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|a Hirano-Iwata, Ayumi
|e verfasserin
|4 aut
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|a Miyamoto, Ko-ichiro
|e verfasserin
|4 aut
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|a Kimura, Yasuo
|e verfasserin
|4 aut
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|a Kataoka, Masatoshi
|e verfasserin
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|a Shinohara, Yasuo
|e verfasserin
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|a Niwano, Michio
|e verfasserin
|4 aut
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 23(2007), 24 vom: 20. Nov., Seite 12287-92
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
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|g volume:23
|g year:2007
|g number:24
|g day:20
|g month:11
|g pages:12287-92
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