Electrolyte-Gated Organic Field-Effect Transistor for Monitoring Amyloid Aggregation

Amyloid-β peptide aggregation is a crucial process in neurological disorders such as Alzheimer’s and Parkinson’s diseases. Amyloids tend to assemble first into oligomers and, subsequently, into larger fibrils. The oligomer species are regarded as the primary cause of neurological dysfunction, and he...

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Detalles Bibliográficos
Autores: Ruiz Molina, Sara, Martínez Domingo, Carme, Ricci, Simona, Casalini, Stefano, Mas Torrent, Marta
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2024
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/382090
Acceso en línea:http://hdl.handle.net/10261/382090
https://api.elsevier.com/content/abstract/scopus_id/85212130782
Access Level:acceso abierto
Palabra clave:Alzheimer’s disease
Electrochemistry
Electrolyte-gated organic field-effect transistor
Protein aggregation
β-amyloid oligomers
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spelling Electrolyte-Gated Organic Field-Effect Transistor for Monitoring Amyloid AggregationRuiz Molina, SaraMartínez Domingo, CarmeRicci, SimonaCasalini, StefanoMas Torrent, MartaAlzheimer’s diseaseElectrochemistryElectrolyte-gated organic field-effect transistorProtein aggregationβ-amyloid oligomersAmyloid-β peptide aggregation is a crucial process in neurological disorders such as Alzheimer’s and Parkinson’s diseases. Amyloids tend to assemble first into oligomers and, subsequently, into larger fibrils. The oligomer species are regarded as the primary cause of neurological dysfunction, and hence, they are key biomarkers for diagnosis and therapy. However, this aggregation process is complex to study, typically requiring the use of a combination of techniques and labeling of the biomolecules. Here, we demonstrate that the electrolyte-gated organic field-effect transistor (EGOFET) device is a promising low-cost transducer that can be used to monitor amyloid aggregation using an electrical readout and without the need of labeling. For this purpose, the gold surface of the gate contact was modified with an amyloid-β 1-40 (Aβ1-40) oligomer-specific antibody using cysteine-protein G (cys-PG). The bioengineered Au electrode was implemented as a recognition element to monitor the aggregation kinetics of Aβ1-40, employing two complementary detection measurements: EGOFET and electrochemical impedance spectroscopy (EIS). The maximum amount of oligomer species was detected after 1 h of incubation. Additionally, dynamic light scattering (DLS) data corroborated these results. More broadly, this work shows the potential of EGOFETs as a label-free platform for studying in vitro protein aggregation, which could be appealing in the future for exploring systematically the experimental parameters affecting the aggregation process or for the development of medical treatments that target the reduction of such aggregation.This work was funded by MCIN/AEI/10.13039/501100011033/ERDF,UE with project SENSATION PID2022-141393OB-I00, and through the “Severo Ochoa” Programme for Centers of Excellence in R&D (CEX2023-001263-S) and the Generalitat de Catalunya (2021-SGR-00443). S.R.-M. is enrolled in the UAB Chemistry Ph.D. S.C. acknowledges two national projects: (i) “Nanochemistry for Energy and Health, NexuS” and (ii) “Complessità Chimica C2” funded by the Italian Ministry of Education, Universities and Research within the funding network termed “Dipartimenti di Eccellenza.” S.C. also acknowledges financial support from the University of Padova through grant P-DiSC#11NexuS_BIRD2020-UNIPD (CARBON-FET).With funding from the Spanish government through the ‘Severo Ochoa Centre of Excellence’ accreditation (CEX2023-001263-S).Peer reviewedAmerican Chemical SocietyMinisterio de Ciencia e Innovación (España)Agencia Estatal de Investigación (España)Generalitat de CatalunyaMinistero dell'Istruzione, dell'Università e della RicercaUniversità degli Studi di PadovaCasalini, Stefano [0000-0003-3609-1154]Mas Torrent, Marta [0000-0002-1586-005X]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202520252024info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/382090https://api.elsevier.com/content/abstract/scopus_id/85212130782reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-141393OB-I00info:eu-repo/grantAgreement/AEI/Plan Estatal de investigación Científica y Técnica y de Innovación 2021-2023/CEX2023-001263-SACS Applied Electronic Materialshttp://doi.org/10.1021/acsaelm.4c01673Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3820902026-05-22T06:33:51Z
dc.title.none.fl_str_mv Electrolyte-Gated Organic Field-Effect Transistor for Monitoring Amyloid Aggregation
title Electrolyte-Gated Organic Field-Effect Transistor for Monitoring Amyloid Aggregation
spellingShingle Electrolyte-Gated Organic Field-Effect Transistor for Monitoring Amyloid Aggregation
Ruiz Molina, Sara
Alzheimer’s disease
Electrochemistry
Electrolyte-gated organic field-effect transistor
Protein aggregation
β-amyloid oligomers
title_short Electrolyte-Gated Organic Field-Effect Transistor for Monitoring Amyloid Aggregation
title_full Electrolyte-Gated Organic Field-Effect Transistor for Monitoring Amyloid Aggregation
title_fullStr Electrolyte-Gated Organic Field-Effect Transistor for Monitoring Amyloid Aggregation
title_full_unstemmed Electrolyte-Gated Organic Field-Effect Transistor for Monitoring Amyloid Aggregation
title_sort Electrolyte-Gated Organic Field-Effect Transistor for Monitoring Amyloid Aggregation
dc.creator.none.fl_str_mv Ruiz Molina, Sara
Martínez Domingo, Carme
Ricci, Simona
Casalini, Stefano
Mas Torrent, Marta
author Ruiz Molina, Sara
author_facet Ruiz Molina, Sara
Martínez Domingo, Carme
Ricci, Simona
Casalini, Stefano
Mas Torrent, Marta
author_role author
author2 Martínez Domingo, Carme
Ricci, Simona
Casalini, Stefano
Mas Torrent, Marta
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia e Innovación (España)
Agencia Estatal de Investigación (España)
Generalitat de Catalunya
Ministero dell'Istruzione, dell'Università e della Ricerca
Università degli Studi di Padova
Casalini, Stefano [0000-0003-3609-1154]
Mas Torrent, Marta [0000-0002-1586-005X]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Alzheimer’s disease
Electrochemistry
Electrolyte-gated organic field-effect transistor
Protein aggregation
β-amyloid oligomers
topic Alzheimer’s disease
Electrochemistry
Electrolyte-gated organic field-effect transistor
Protein aggregation
β-amyloid oligomers
description Amyloid-β peptide aggregation is a crucial process in neurological disorders such as Alzheimer’s and Parkinson’s diseases. Amyloids tend to assemble first into oligomers and, subsequently, into larger fibrils. The oligomer species are regarded as the primary cause of neurological dysfunction, and hence, they are key biomarkers for diagnosis and therapy. However, this aggregation process is complex to study, typically requiring the use of a combination of techniques and labeling of the biomolecules. Here, we demonstrate that the electrolyte-gated organic field-effect transistor (EGOFET) device is a promising low-cost transducer that can be used to monitor amyloid aggregation using an electrical readout and without the need of labeling. For this purpose, the gold surface of the gate contact was modified with an amyloid-β 1-40 (Aβ1-40) oligomer-specific antibody using cysteine-protein G (cys-PG). The bioengineered Au electrode was implemented as a recognition element to monitor the aggregation kinetics of Aβ1-40, employing two complementary detection measurements: EGOFET and electrochemical impedance spectroscopy (EIS). The maximum amount of oligomer species was detected after 1 h of incubation. Additionally, dynamic light scattering (DLS) data corroborated these results. More broadly, this work shows the potential of EGOFETs as a label-free platform for studying in vitro protein aggregation, which could be appealing in the future for exploring systematically the experimental parameters affecting the aggregation process or for the development of medical treatments that target the reduction of such aggregation.
publishDate 2024
dc.date.none.fl_str_mv 2024
2025
2025
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/382090
https://api.elsevier.com/content/abstract/scopus_id/85212130782
url http://hdl.handle.net/10261/382090
https://api.elsevier.com/content/abstract/scopus_id/85212130782
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-141393OB-I00
info:eu-repo/grantAgreement/AEI/Plan Estatal de investigación Científica y Técnica y de Innovación 2021-2023/CEX2023-001263-S
ACS Applied Electronic Materials
http://doi.org/10.1021/acsaelm.4c01673
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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