Biosensors for life quality

Castillo, Jaime; Gáspár, Szilveszter; Leth, Suzanne; Niculescu, Mihaela; Mortari, Alessia; Bontidean, Ibolya; Soukharev, Valentin S; Dorneanu, Sorin-Aurel; Ryabov, Alexander D.; Csöregi, Elisabeth

doi:10.1016/j.snb.2004.04.084

Cited by 226 publications

(83 citation statements)

References 106 publications

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“…For example, because of the affinity and specificity of biomolecular recognition, biosensors often exhibit impressive sensitivity and selectivity relative to nonbiological approaches (2,3). Furthermore, because high-affinity proteins can be produced in the laboratory that specifically bind almost any water-soluble ligand (4-6), a generic, protein-based biosensor platform should be highly generalizable.…”

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confidence: 99%

“…Furthermore, because high-affinity proteins can be produced in the laboratory that specifically bind almost any water-soluble ligand (4-6), a generic, protein-based biosensor platform should be highly generalizable. Despite these advantages, however, the application of proteins to commercially viable, real-time electronic or optical biosensors has remained limited, with the glucose oxidase-based glucose sensor being a notable exception (2).…”

mentioning

confidence: 99%

“…A large number of electronic and optical protein-based sensors have been described in the literature, many of which feature impressive sensitivity and generalizability (2,3). Because the physical properties of proteins generally do not change significantly upon ligand binding, however, most of these approaches require the addition of multiple reagents or use changes in relatively nonspecific properties, such as mass, charge, or electron density, to generate an observable signal.…”

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confidence: 99%

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Engineering a signal transduction mechanism for protein-based biosensors

Kohn

Plaxco

2005

Proc. Natl. Acad. Sci. U.S.A.

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Hybridization-induced conformational changes have been successfully used in biosensors for the transduction of DNA-binding events into readily observable optical or electronic signals. Similar signal transduction has not, however, proven of equal utility in proteinbased biosensors. The discrepancy arises because, unlike ssDNA, most proteins do not undergo significant conformational changes upon ligand binding. Here, we describe a solution to this problem. We show that an arbitrarily selected, normally well folded protein can be rationally engineered such that it undergoes ligand-induced folding. The engineered protein responds rapidly (milliseconds) and selectively to its target, and it couples recognition with the largest possible conformational change: folding. These traits suggest that ligand-induced folding could serve as an ideal signaltransduction mechanism. Consistent with this claim, we demonstrate a label-free optical biosensor based on the effect that is sufficiently selective to detect its target even in complex, contaminant-ridden samples such as blood serum.fluorescence ͉ molecular beacon ͉ natively unfolded ͉ quenching

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Engineering a signal transduction mechanism for protein-based biosensors

Kohn

Plaxco

2005

Proc. Natl. Acad. Sci. U.S.A.

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“…Nowadays, biosensors are widely applied for the detection, identification, and characterization of biological material, which is of great importance in industrial (Castillo et al, 2004), medical (Hsieh et al, 2004;Dillon et al, 2005;Jiang et al, 2005), food (Gustavsson et al, 2002;Haasnoot et al, 2002;Indyk and Filonzi, 2005;Muller-Renaud et al, 2005), and environmental (Castillo et al, 2004) analysis. Surface plasmon resonance-based biosensors are currently widely used to monitor these interactions (Chou et al, 2004;Oh et al, 2004;Choi et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

The application of neoglycopeptides in the development of sensitive surface plasmon resonance-based biosensors

Maljaars

Souza

Halkes

et al. 2008

Biosensors and Bioelectronics

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a b s t r a c tThe development of a biosensor based on surface plasmon resonance is described for the detection of carbohydrate-binding proteins in solution on a Biacore 2000 instrument, using immobilized glycopeptides as ligands. Their selection was based on previous screenings of solid-phase glycopeptide libraries with Ricinus communis agglutinin (RCA 120 ) and human adhesion/growth-regulatory galectin-1 (h-Gal-1). Glycopeptides were immobilized on Au sensor chips functionalized with mixed self-assembled monolayers of different ratios of 11-mercapto-1-undecanol and 11-mercaptoundecanoic acid, and of 3-mercapto-1-propanol and 11-mercaptoundecanoic acid. The biosensors were optimized for the detection of RCA 120 , and a detection limit of 0.13 nM was obtained. Subsequent experiments with h-Gal-1 indicated a detection limit of at least 0.9 nM for this lectin. Additionally, the effect of interfering proteins on the sensitivity of the optimized biosensor was investigated.

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“…The selectivity of the biosensor for the target analyte is mainly determined by the biorecognition element, while the selectivity of the biosensor is greatly influenced by the transducer [1]. Very often the biorecognition elements are enzymes [2] and a good functioning of an electrochemical enzyme biosensor requires a redox mediator, which shuttles electrons between the recognition element and the transducer and reduces interferences since lower applied potentials can be employed.…”

Section: Introductionmentioning

confidence: 99%

Design and application of a flow cell for carbon-film based electrochemical enzyme biosensors

Bârsan

Klincar

Batič

et al. 2007

Talanta

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A flow cell has been designed for use with an electrochemical enzyme biosensor, based on low-cost carbon-film electrodes. Three types of mediators were used: cobalt and copper hexacyanoferrates and poly(neutral red) (PNR), covered with glucose oxidase (GOx) immobilised by cross-linking with glutaraldehyde in the presence of bovine serum albumin or inside a oxysilane sol-gel network. Mixtures of sol-gel precursors were made from 3-aminopropyl-triethoxysilane (APTOS) together with methyltrimethoxysilane (MTMOS), methyltriethoxysilane (MTEOS), tetraethyloxysilane (TEOS) or 3-glycidoxypropyl-trimethoxysilane (GOPMOS), and the best chosen for encapsulation. Optimisation in batch mode, using amperometric detection at fixed potential, showed the PNR-GOx modified carbon-film electrodes to be best for flow analysis for both glutaraldehyde and sol-gel enzyme immobilisation. Both types of enzyme electrode were tested under flow conditions and the reproducibility and stability of the biosensors were evaluated. The biosensors were used for fermentation monitoring of glucose in grape must and interference studies were also performed.

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Biosensors for life quality

Cited by 226 publications

References 106 publications

Engineering a signal transduction mechanism for protein-based biosensors

Engineering a signal transduction mechanism for protein-based biosensors

The application of neoglycopeptides in the development of sensitive surface plasmon resonance-based biosensors

Design and application of a flow cell for carbon-film based electrochemical enzyme biosensors

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