Imidazolium-Based Ionic Liquid Surfaces for Biosensing

Ionic liquid self-assembled monolayers (SAM) were designed and applied for binding streptavidin, promoting affinity biosensing and enzyme activity on gold surfaces of sensors. The synthesis of 1-((+)-biotin)pentanamido)propyl)-3-(12-mercaptododecyl)-imidazolium bromide, a biotinylated ionic liquid (...

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Bibliographic Details
Published in:Analytical chemistry (Washington) 2013-06, Vol.85 (12), p.5770-5777
Main Authors: Ratel, Mathieu, Provencher-Girard, Audrey, Zhao, Sandy Shuo, Breault-Turcot, Julien, Labrecque-Carbonneau, Jérémie, Branca, Mathieu, Pelletier, Joelle N, Schmitzer, Andreea R, Masson, Jean-Francois
Format: Article
Language:English
Subjects:
Affinity
Biosensing Techniques - methods
Biosensors
Chelating
Enzyme activity
Enzymes
Gold
Humans
Imidazoles - chemistry
Immunoglobulins
Ionic liquids
Ionic Liquids - chemistry
Polyethylene glycol
Sensors
Surface chemistry
Surface Plasmon Resonance - methods
Synthesis
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Summary:Ionic liquid self-assembled monolayers (SAM) were designed and applied for binding streptavidin, promoting affinity biosensing and enzyme activity on gold surfaces of sensors. The synthesis of 1-((+)-biotin)pentanamido)propyl)-3-(12-mercaptododecyl)-imidazolium bromide, a biotinylated ionic liquid (IL-biotin), which self-assembles on gold film, afforded streptavidin sensing with surface plasmon resonance (SPR). The IL-biotin-SAM efficiently formed a full streptavidin monolayer. The synthesis of 1-(carboxymethyl)-3-(mercaptododecyl)-imidazoliumbromide, a carboxylated IL (IL-COOH), was used to immobilize anti-IgG to create an affinity biosensor. The IL-COOH demonstrated efficient detection of IgG in the nanomolar concentration range, similar to the alkylthiols SAM and PEG. In addition, the IL-COOH demonstrated low fouling in crude serum, to a level equivalent to PEG. The IL-COOH was further modified with N,N′-bis (carboxymethyl)-l-lysine hydrate to bind copper ions and then, chelate histidine-tagged biomolecules. Human dihydrofolate reductase (hDHFR) was chelated to the modified IL-COOH. By monitoring enzyme activity in situ on the SPR sensor, it was revealed that the IL-COOH SAM improved the activity of hDHFR by 24% in comparison to classical SAM. Thereby, IL-SAM has been synthesized and successfully applied to three important biosensing schemes, demonstrating the advantages of this new class of monolayers.
ISSN:0003-2700
1520-6882
DOI:10.1021/ac400386z