Emerging applications of aptamers to micro- and nanoscale biosensing

Nguyen, Thai; Hilton, John P.; Lin, Qiao

doi:10.1007/s10404-008-0400-7

Cited by 52 publications

(30 citation statements)

References 141 publications

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“…To date, much of the work with CE and optical biosensors has focused on aptamers or nucleic acid molecular beacons for target detection, typically with a mobility shift for the aptamer [3][4][5][6]. In this study, we show that affinity capillary electrophoresis (ACE) can be used to measure peptide specificity and binding affinity of a synthetic peptide selected from a bacterial display library to bind exclusively to PA of B. anthracis.…”

Section: Introductionmentioning

confidence: 92%

Binding specificity and affinity analysis of an anti-protective antigen peptide reagent using capillary electrophoresis

Kogot¹,

Sarkes²,

Pennington³

et al. 2014

ABB

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Peptide biosensor reagents are emerging as an alternative to typical antibody-based detection methods. Peptides can be rapidly isolated using bacterial display methods for new and emerging biothreats and can be chemically synthesized for rapid, large-scale production. With the emergence of peptide biosensor reagents, there is a growing need to develop methods for characterizing binding interactions. Capillary electrophoresis (CE) is a free-solution separation method that is able to determine target and analyte binding association (K b ) and dissociation constants (K d ). In this study, the K b , K d , and peptide specificity of an isolated peptide binding reagent to protective antigen (PA) of Bacillus anthracis were evaluated using capillary electrophoresis at 10 and 20 kV. The relative binding specificity was rapidly assessed by measuring the peptide relative mobility shift at 20 kV at nonequilibrium using bovine serum albumin (BSA), horseradish peroxidase (HRP), and an anti-PA monoclonal antibody (mAb). The αPA peptide was shown to be highly specific for PA, with a K d = 177 nM measured at 20 kV and K d = 312 nM measured at 10 kV. These results show that peptides from bacterial display libraries can be rapidly tested for specificity and binding affinity, in solution, for use as a potential biosensor reagent against new and emerging biothreats.

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Section: Introductionmentioning

confidence: 92%

Binding specificity and affinity analysis of an anti-protective antigen peptide reagent using capillary electrophoresis

Kogot¹,

Sarkes²,

Pennington³

et al. 2014

ABB

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“…Altogether these properties make aptamers an appropriate tool in the development of aptasensors (de-los-Santos-Álvarez et al, 2008;Guo et al, 2008;Hianik and Wang, 2009;Lee et al, 2008;Park et al, 2009;Song et al, 2008Song et al, , 2012Tombelli et al, 2005;Velasco-Garcia and Missailidis, 2009;Zhang and Chen, 2010). Additional advantages include the possibility of performing several analysis with mild changes of the binding specificity and selectivity; along with the possibility of using different designs and detection strategies for fast and easy detection of protein in real biological samples Hianik and Wang, 2009;Hianik et al, 2007;Kim et al, 2008;Nguyen et al, 2009;Song et al, 2008;Zhou et al, 2011). The lack of specific aptamers for the majority of protein disease biomarkers, as well as the existence of few aptamers with two recognition sites for a single target, may limit the development of aptasensors.…”

Section: Aptamer-based Biosensors: Aptasensorsmentioning

confidence: 99%

Voltammetric aptasensors for protein disease biomarkers detection: A review

Meirinho

Dias

Peres

et al. 2016

Biotechnology Advances

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An electrochemical aptasensor is a compact analytical device where the bioreceptor (aptamer) is coupled to a transducer surface to convert a biological interaction into a measurable signal (current) that can be easily processed, recorded and displayed. Since the discovery of the Systematic Evolution of Ligands by Enrichment (SELEX) methodology, the selection of aptamers and their application as bioreceptors has become a promising tool in the design of electrochemical aptasensors. Aptamers present several advantages that highlight their usefulness as bioreceptors such as chemical stability, cost effectiveness and ease of modification towards detection and immobilization at different transducer surfaces. In this review, a special emphasis is given to the potential use of electrochemical aptasensors for the detection of protein disease biomarkers using voltammetry techniques. Methods for the immobilization of aptamers onto electrode surfaces are discussed, as well as different electrochemical strategies that can be used for the design of aptasensors.

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“…Biomolecular affinity binding is of fundamental importance for a wide variety of biological processes in that conformational and chemical complementarity between the binding molecules strongly influences cellular signal transduction and expression [1]. Modern drug development and therapeutics have thus increasingly relied on biomolecular binding studies [2]; current experimental and computational screening of compounds for therapeutic drugs is often based on interrogation of ligand-receptor binding affinity [3].…”

Section: Introductionmentioning

confidence: 99%

Microcantilever-based label-free characterization of temperature-dependent biomolecular affinity binding

Wang

Huang

Nguyen

et al. 2013

Sensors and Actuators B: Chemical

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This paper presents label-free characterization of temperature-dependent biomolecular affinity binding on solid surfaces using a microcantilever-based device. The device consists of a Parylene cantilever one side of which is coated with a gold film and functionalized with molecules as an affinity receptor to a target analyte. The cantilever is located in a poly(dimethylsiloxane) (PDMS) microfluidic chamber that is integrated with a transparent indium tin oxide (ITO) resistive temperature sensor on the underlying substrate. The ITO sensor allows for real-time measurements of the chamber temperature, as well as unobstructed optical access for reflection-based optical detection of the cantilever deflection. To test the temperature-dependent binding between the target and receptor, the temperature of the chamber is maintained at a constant setpoint, while a solution of unlabeled analyte molecules is continuously infused through the chamber. The measured cantilever deflection is used to determine the target-receptor binding characteristics. We demonstrate label-free characterization of temperature-dependent binding kinetics of the platelet-derived growth factor (PDGF) protein with an aptamer receptor. Affinity binding properties including the association and dissociation rate constants as well as equilibrium dissociation constant are obtained, and shown to exhibit significant dependencies on temperature.

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Emerging applications of aptamers to micro- and nanoscale biosensing

Cited by 52 publications

References 141 publications

Binding specificity and affinity analysis of an anti-protective antigen peptide reagent using capillary electrophoresis

Binding specificity and affinity analysis of an anti-protective antigen peptide reagent using capillary electrophoresis

Voltammetric aptasensors for protein disease biomarkers detection: A review

Microcantilever-based label-free characterization of temperature-dependent biomolecular affinity binding

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