Identification of high-affinity phage-displayed V<inf>H</inf> fragments by use of a quartz crystal microbalance with dissipation monitoring
10 Pág. Departamento de Tecnología de Alimentos
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| Format: | artículo biblioteca |
| Language: | English |
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Elsevier
2021-08-01
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| Subjects: | Antibody fragment, Biosensor, Lectins, Phage display, Principal component analysis, Quartz crystal microbalance, |
| Online Access: | http://hdl.handle.net/10261/288569 http://dx.doi.org/10.13039/501100000780 http://dx.doi.org/10.13039/501100004837 https://api.elsevier.com/content/abstract/scopus_id/85104330019 |
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dig-inia-es-10261-2885692024-10-27T22:01:47Z Identification of high-affinity phage-displayed V<inf>H</inf> fragments by use of a quartz crystal microbalance with dissipation monitoring Gómez-Arribas, Lidia N. Juste-Dolz, Augusto Peltomaa, Riikka Giménez-Romero, David Morais, Sergi Barderas, Rodrigo Cuadrado Hoyos, María Carmen Maquieira, Ángel Benito-Peña, Elena Moreno-Bondi, María C. Ministerio de Ciencia e Innovación (España) European Commission Juste-Dolz, Augusto [0000-0003-4889-6419] Giménez-Romero, David [0000-0001-6489-9308] Morais, Sergi [0000-0002-3722-2358] Barderas, Rodrigo [0000-0003-3539-7469] Cuadrado Hoyos, María Carmen [0000-0003-2609-1900] Maquieira, Ángel [0000-0003-4641-4957] Benito-Peña, Elena [0000-0001-5685-5559] Moreno-Bondi, María C. [0000-0002-3612-0675] Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72] Antibody fragment Biosensor Lectins Phage display Principal component analysis Quartz crystal microbalance 10 Pág. Departamento de Tecnología de Alimentos 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 phage-displayed 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 high-affinity 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. 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). Peer reviewed 2023-02-08T07:49:42Z 2023-02-08T07:49:42Z 2021-08-01 artículo http://purl.org/coar/resource_type/c_6501 Sensors and Actuators - B - Chemical Biochemical Sensors 340:129954 (2021) 0925-4005 http://hdl.handle.net/10261/288569 10.1016/j.snb.2021.129954 http://dx.doi.org/10.13039/501100000780 http://dx.doi.org/10.13039/501100004837 2-s2.0-85104330019 https://api.elsevier.com/content/abstract/scopus_id/85104330019 en #PLACEHOLDER_PARENT_METADATA_VALUE# #PLACEHOLDER_PARENT_METADATA_VALUE# #PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/RTI2018-096410-B-C21/ES/MATERIALES BIO(MIMETICOS) INNOVADORES PARA SENSORES OPTICOS Y SEPARACIONES ANALITICAS/ info:eu-repo/grantAgreement/MICINN//CTQ2016-75749-R info:eu-repo/grantAgreement/EC//2020/094 Sensors and Actuators, B: Chemical Publisher's version https://doi.org/10.1016/j.snb.2021.129954 Sí open Elsevier |
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Antibody fragment Biosensor Lectins Phage display Principal component analysis Quartz crystal microbalance Antibody fragment Biosensor Lectins Phage display Principal component analysis Quartz crystal microbalance |
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Antibody fragment Biosensor Lectins Phage display Principal component analysis Quartz crystal microbalance Antibody fragment Biosensor Lectins Phage display Principal component analysis Quartz crystal microbalance Gómez-Arribas, Lidia N. Juste-Dolz, Augusto Peltomaa, Riikka Giménez-Romero, David Morais, Sergi Barderas, Rodrigo Cuadrado Hoyos, María Carmen Maquieira, Ángel Benito-Peña, Elena Moreno-Bondi, María C. Identification of high-affinity phage-displayed V<inf>H</inf> fragments by use of a quartz crystal microbalance with dissipation monitoring |
| description |
10 Pág.
Departamento de Tecnología de Alimentos |
| author2 |
Ministerio de Ciencia e Innovación (España) |
| author_facet |
Ministerio de Ciencia e Innovación (España) Gómez-Arribas, Lidia N. Juste-Dolz, Augusto Peltomaa, Riikka Giménez-Romero, David Morais, Sergi Barderas, Rodrigo Cuadrado Hoyos, María Carmen Maquieira, Ángel Benito-Peña, Elena Moreno-Bondi, María C. |
| format |
artículo |
| topic_facet |
Antibody fragment Biosensor Lectins Phage display Principal component analysis Quartz crystal microbalance |
| author |
Gómez-Arribas, Lidia N. Juste-Dolz, Augusto Peltomaa, Riikka Giménez-Romero, David Morais, Sergi Barderas, Rodrigo Cuadrado Hoyos, María Carmen Maquieira, Ángel Benito-Peña, Elena Moreno-Bondi, María C. |
| author_sort |
Gómez-Arribas, Lidia N. |
| title |
Identification of high-affinity phage-displayed V<inf>H</inf> fragments by use of a quartz crystal microbalance with dissipation monitoring |
| title_short |
Identification of high-affinity phage-displayed V<inf>H</inf> fragments by use of a quartz crystal microbalance with dissipation monitoring |
| title_full |
Identification of high-affinity phage-displayed V<inf>H</inf> fragments by use of a quartz crystal microbalance with dissipation monitoring |
| title_fullStr |
Identification of high-affinity phage-displayed V<inf>H</inf> fragments by use of a quartz crystal microbalance with dissipation monitoring |
| title_full_unstemmed |
Identification of high-affinity phage-displayed V<inf>H</inf> fragments by use of a quartz crystal microbalance with dissipation monitoring |
| title_sort |
identification of high-affinity phage-displayed v<inf>h</inf> fragments by use of a quartz crystal microbalance with dissipation monitoring |
| publisher |
Elsevier |
| publishDate |
2021-08-01 |
| url |
http://hdl.handle.net/10261/288569 http://dx.doi.org/10.13039/501100000780 http://dx.doi.org/10.13039/501100004837 https://api.elsevier.com/content/abstract/scopus_id/85104330019 |
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