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Identification of high-affinity phage-displayed VH fragments by use of a quartz crystal microbalance with dissipation monitoring

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Identification of high-affinity phage-displayed VH fragments by use of a quartz crystal microbalance with dissipation monitoring

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dc.contributor.author Gómez-Arribas, Lidia N. es_ES
dc.contributor.author Juste-Dolz, Augusto Miguel es_ES
dc.contributor.author Peltomaa, Riikka es_ES
dc.contributor.author Giménez-Romero, David es_ES
dc.contributor.author Morais, Sergi es_ES
dc.contributor.author Barderas, Rodrigo es_ES
dc.contributor.author Cuadrado, Carmen es_ES
dc.contributor.author Maquieira Catala, Angel es_ES
dc.contributor.author Benito-Peña, Elena es_ES
dc.contributor.author Moreno-Bondi, María C. es_ES
dc.date.accessioned 2023-06-07T18:01:13Z
dc.date.available 2023-06-07T18:01:13Z
dc.date.issued 2021-08-01 es_ES
dc.identifier.issn 0925-4005 es_ES
dc.identifier.uri http://hdl.handle.net/10251/193935
dc.description.abstract [EN] Phage display has become a powerful tool for antibody discovery in a wide variety of fields. This technology allows specific binders for a given antigen to be selected from combinatorial libraries. A key step in the process is characterizing and evaluating antibody clones thus selected to reliably identify the best antigen binders. Novel characterization methods can provide essential insight into the binding mechanism and supplement the information obtained with conventional techniques. In this work, we used a quartz crystal microbalance with dissipation monitoring (QCM-D) to determine the kinetic and thermodynamic binding parameters for phagedisplayed VH antibody fragments. Phytohemagglutinin (PHA), a legume lectin of analytical interest, was used as a complex model antigen to select specific VH fragments from a phage-displayed library. Eight VH fragments with a unique amino acid sequence were identified as PHA binders by using the well-established enzyme-linked immunosorbent assay (ELISA). QCM-D measurements, structural analysis and principal component analysis (PCA) were used to evaluate the antibody fragments and identify clone clusters with similar binding characteristics and molecular interaction mechanisms. This unprecedented study has enabled the identification of highaffinity phage-displayed VH antibody fragments for PHA, which could be useful for PHA analysis (apparent association constant ranged from 108 to 1010 M-1). In fact, the proposed methodology provides a useful tool for evaluating and characterizing antibody fragments with capabilities beyond those of conventional techniques es_ES
dc.description.sponsorship This work was funded by the Spanish Ministry of Science and Innovation and the Spanish Ministry of Economy and Competitiveness (Projects RTI2018-096410-B-C21 and CTQ2016-75749-R, respectively), GVA's Prometeo program (Grant 2020/094) and the European Regional Development Fund (ERDF). es_ES
dc.language Inglés es_ES
dc.publisher Elsevier es_ES
dc.relation.ispartof Sensors and Actuators B Chemical es_ES
dc.rights Reserva de todos los derechos es_ES
dc.subject Phage display es_ES
dc.subject Antibody fragment es_ES
dc.subject Quartz crystal microbalance es_ES
dc.subject Biosensor es_ES
dc.subject Principal component analysis es_ES
dc.subject Lectins es_ES
dc.subject.classification QUIMICA ANALITICA es_ES
dc.title Identification of high-affinity phage-displayed VH fragments by use of a quartz crystal microbalance with dissipation monitoring es_ES
dc.type Artículo es_ES
dc.identifier.doi 10.1016/j.snb.2021.129954 es_ES
dc.relation.projectID info:eu-repo/grantAgreement/AEI//CTQ2016-75749-R//BIOSENSORES HOLOGRAFICOS. PRUEBA DE CONCEPTO Y DEMOSTRACION EN APLICACIONES CLINICAS/ es_ES
dc.relation.projectID info:eu-repo/grantAgreement/GENERALITAT VALENCIANA//PROMETEO%2F2020%2F094//HOLOGRAFÍA. UNA VIA PARA AFRONTAR NUEVOS RETOS EN BIOSENSADO/ es_ES
dc.relation.projectID info:eu-repo/grantAgreement/MICINN//RTI2018-096410-B-C21/ es_ES
dc.rights.accessRights Cerrado es_ES
dc.contributor.affiliation Universitat Politècnica de València. Escuela Técnica Superior de Ingeniería Agronómica y del Medio Natural - Escola Tècnica Superior d'Enginyeria Agronòmica i del Medi Natural es_ES
dc.description.bibliographicCitation Gómez-Arribas, LN.; Juste-Dolz, AM.; Peltomaa, R.; Giménez-Romero, D.; Morais, S.; Barderas, R.; Cuadrado, C.... (2021). Identification of high-affinity phage-displayed VH fragments by use of a quartz crystal microbalance with dissipation monitoring. Sensors and Actuators B Chemical. 340:1-10. https://doi.org/10.1016/j.snb.2021.129954 es_ES
dc.description.accrualMethod S es_ES
dc.relation.publisherversion https://doi.org/10.1016/j.snb.2021.129954 es_ES
dc.description.upvformatpinicio 1 es_ES
dc.description.upvformatpfin 10 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 340 es_ES
dc.relation.pasarela S\435187 es_ES
dc.contributor.funder GENERALITAT VALENCIANA es_ES
dc.contributor.funder AGENCIA ESTATAL DE INVESTIGACION es_ES
dc.contributor.funder European Regional Development Fund es_ES
dc.contributor.funder Ministerio de Ciencia e Innovación es_ES


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