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231225s2019 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.8b03898
|2 doi
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|a pubmed24n0974.xml
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|e rakwb
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|a eng
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| 100 |
1 |
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|a Gao, Su
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Real-Time Profiling of Anti-(Epithelial Cell Adhesion Molecule)-Based Immune Capture from Molecules to Cells Using Multiparameter Surface Plasmon Resonance
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|c 2019
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|a ƒa Online-Ressource
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|a Date Completed 05.06.2019
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|a Date Revised 05.06.2019
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Antibodies of epithelial cell-adhesion molecule (anti-EpCAM)-based interfaces have proven to be highly efficient at capturing circulating tumor cells (CTCs). To achieve the bonding of anti-EpCAM to the interface, biotin and streptavidin are used to modify the surface. These processes are critical to subsequent cell-capture efficiencies. However, quantitative research on the interactions between biotin, streptavidin, and biotinylated anti-EpCAM on the interface is lacking. In this work, the thermodynamics and kinetics of biomolecular interactions were determined by using surface plasmon resonance. The equilibrium binding affinities for biotinylated anti-EpCAM to streptavidin and streptavidin to biotin (illustrated by biotin-PEG400-thiol) were found to be 2.75 × 106 and 8.82 × 106 M-1, respectively. Each streptavidin can bind up to 2.30 biotinylated anti-EpCAM under thermodynamic equilibrium. The findings provide useful information to optimize the modification of anti-EpCAM and improve the capture efficiency of CTCs
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Antibodies
|2 NLM
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|a Epithelial Cell Adhesion Molecule
|2 NLM
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| 650 |
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|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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|a Streptavidin
|2 NLM
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| 650 |
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|a 9013-20-1
|2 NLM
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| 700 |
1 |
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|a Chen, Shuangshuang
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Lu, Qinghua
|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 35(2019), 4 vom: 29. Jan., Seite 1040-1046
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
1 |
8 |
|g volume:35
|g year:2019
|g number:4
|g day:29
|g month:01
|g pages:1040-1046
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| 856 |
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|u http://dx.doi.org/10.1021/acs.langmuir.8b03898
|3 Volltext
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