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Carbohydrate-Mediated Biomolecular Recognition and Gating of Synthetic Ion Channels

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Carbohydrate-Mediated Biomolecular Recognition and Gating of Synthetic Ion Channels

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dc.contributor.author Ali, Mubarak es_ES
dc.contributor.author Nasir, Saima es_ES
dc.contributor.author Ramirez Hoyos, Patricio es_ES
dc.contributor.author Cervera Montesinos, Javier es_ES
dc.contributor.author Mafe, Salvador es_ES
dc.contributor.author Ensinger, Wolfgang es_ES
dc.date.accessioned 2014-06-25T10:45:29Z
dc.date.issued 2013-09-05
dc.identifier.issn 1932-7447
dc.identifier.uri http://hdl.handle.net/10251/38360
dc.description.abstract Nanochannel-based biosensing devices have been proposed for selective detection of protein analyte molecules. However, the design and miniaturization of reusable channel-based biosensors is still a challenge in nanoscience and biotechnology. We present here a reusable nanofluidic biosensor based on reversible lectin-carbohydrate interactions. The nanochannels are fabricated in heavy ion tracked polymer membranes. The channel walls are functionalized with p-aminophenyl alpha-D-mannopyranoside (APMP) monolayers through carbodiimide coupling chemistry. The chemical (mannopyranoside) groups on the inner channel walls serve as binding sites and interact with specific protein molecules. The binding (bioconjugation)/unbinding of proteins inside the confined geometry gives measurable changes in the electrical conductance for the case of single channel and in the permeation rate for a multichannel membrane. The modified-channel selectively recognizes concanavalin A (ConA) protein, but not the control proteins (lysozyme and bovine serum albumin), because ConA specifically binds with the mannopyranoside moieties. The method permits ConA detection in the range 10 nM to 1000 nM. Moreover, the ConA binding/unbinding is reversible, allowing several measuring cycles by washing the bioconjugated-channels with mannose solution. The experimental results are explained qualitatively by introducing a phenomenological model that incorporates the basic experimental trends observed in the current-voltage curves. es_ES
dc.description.sponsorship M.A., S.N., and W.E. acknowledge the Beilstein-Institut, Frankfurt/Main, Germany, within the research collaboration NanoBiC. P.R., J.C., and S.M. acknowledge the Ministry of Economic Affairs and Competitiveness and FEDER (Project MAT2012-32084) as well as the Generalitat Valenciana (Project PROMETEO/GV/0069). The authors thank Prof. Christina Trautmann from GSI for support with the heavy ion irradiation experiments. en_EN
dc.format.extent 9 es_ES
dc.language Inglés es_ES
dc.publisher American Chemical Society es_ES
dc.relation FEDER (Project MAT2012-32084) es_ES
dc.relation Generalitat Valenciana (Project PROMETEO/GV/0069) es_ES
dc.relation.ispartof Journal of Physical Chemistry C es_ES
dc.rights Reserva de todos los derechos es_ES
dc.subject Dna analysis es_ES
dc.subject Cell recognition es_ES
dc.subject Nanofluidic diode es_ES
dc.subject Asymmetric nanopores es_ES
dc.subject Concanavalin A es_ES
dc.subject Solid state nanopores es_ES
dc.subject Saccharide binding site es_ES
dc.subject Mannose labeled enzymes es_ES
dc.subject Self assembled monolayers es_ES
dc.subject.classification FISICA APLICADA es_ES
dc.title Carbohydrate-Mediated Biomolecular Recognition and Gating of Synthetic Ion Channels es_ES
dc.type Artículo es_ES
dc.embargo.lift 10000-01-01
dc.embargo.terms forever es_ES
dc.identifier.doi 10.1021/jp4054555
dc.rights.accessRights Cerrado es_ES
dc.contributor.affiliation Universitat Politècnica de València. Departamento de Física Aplicada - Departament de Física Aplicada es_ES
dc.description.bibliographicCitation Ali, M.; Nasir, S.; Ramirez Hoyos, P.; Cervera Montesinos, J.; Mafe, S.; Ensinger, W. (2013). Carbohydrate-Mediated Biomolecular Recognition and Gating of Synthetic Ion Channels. Journal of Physical Chemistry C. 117(35):18234-18242. doi:10.1021/jp4054555 es_ES
dc.description.accrualMethod Senia es_ES
dc.relation.publisherversion http://dx.doi.org/10.1021/jp4054555 es_ES
dc.description.upvformatpinicio 18234 es_ES
dc.description.upvformatpfin 18242 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 117 es_ES
dc.description.issue 35 es_ES
dc.relation.senia 255520


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