Paper-Based Platform with an In Situ Molecularly Imprinted Polymer for β-Amyloid

Detalhes bibliográficos
Autor(a) principal: Pereira, Marta V.
Data de Publicação: 2020
Outros Autores: Marques, Ana C., Oliveira, Daniela, Martins, Rodrigo, Moreira, Felismina, Sales, Maria Goreti Ferreira, Fortunato, Elvira
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10400.22/18576
Resumo: Alzheimer’s disease (AD) is one of the most common forms of dementia affecting millions of people worldwide. Currently, an easy and effective form of diagnosis is missing, which significantly hinders a possible improvement of the patient’s quality of life. In this context, biosensors emerge as a future solution, opening the doors for preventive medicine and allowing the premature diagnosis of numerous pathologies. This work presents a pioneering biosensor that combines a bottom-up design approach using paper as a platform for the electrochemical recognition of peptide amyloid β-42 (Aβ-42), a biomarker for AD present in blood, associated with visible differences in the brain tissue and responsible for the formation of senile plaques. The sensor layer relies on a molecularly imprinted polymer as a biorecognition element, created on the carbon ink electrode’s surface by electropolymerizing a mixture of the target analyte (Aβ-42) and a monomer (O-phenylenediamine) at neutral pH 7.2. Next, the template molecule was removed from the polymeric network by enzymatic and acidic treatments. The vacant sites so obtained preserved the shape of the imprinted protein and were able to rebind the target analyte. Morphological and chemical analyses were performed in order to control the surface modification of the materials. The analytical performance of the biosensor was evaluated by an electroanalytical technique, namely, square wave voltammetry. For this purpose, the analytical response of the biosensor was tested with standard solutions ranging from 0.1 ng/mL to 1 μg/mL of Aβ-42. The linear response of the biosensor went down to 0.1 ng/mL. Overall, the developed biosensor offered numerous benefits, such as simplicity, low cost, reproducibility, fast response, and repeatability less than 10%. All together, these features may have a strong impact in the early detection of AD.
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spelling Paper-Based Platform with an In Situ Molecularly Imprinted Polymer for β-AmyloidSensorsPeptides and proteinsElectrodesBiotechnologyPolymersAlzheimer’s disease (AD) is one of the most common forms of dementia affecting millions of people worldwide. Currently, an easy and effective form of diagnosis is missing, which significantly hinders a possible improvement of the patient’s quality of life. In this context, biosensors emerge as a future solution, opening the doors for preventive medicine and allowing the premature diagnosis of numerous pathologies. This work presents a pioneering biosensor that combines a bottom-up design approach using paper as a platform for the electrochemical recognition of peptide amyloid β-42 (Aβ-42), a biomarker for AD present in blood, associated with visible differences in the brain tissue and responsible for the formation of senile plaques. The sensor layer relies on a molecularly imprinted polymer as a biorecognition element, created on the carbon ink electrode’s surface by electropolymerizing a mixture of the target analyte (Aβ-42) and a monomer (O-phenylenediamine) at neutral pH 7.2. Next, the template molecule was removed from the polymeric network by enzymatic and acidic treatments. The vacant sites so obtained preserved the shape of the imprinted protein and were able to rebind the target analyte. Morphological and chemical analyses were performed in order to control the surface modification of the materials. The analytical performance of the biosensor was evaluated by an electroanalytical technique, namely, square wave voltammetry. For this purpose, the analytical response of the biosensor was tested with standard solutions ranging from 0.1 ng/mL to 1 μg/mL of Aβ-42. The linear response of the biosensor went down to 0.1 ng/mL. Overall, the developed biosensor offered numerous benefits, such as simplicity, low cost, reproducibility, fast response, and repeatability less than 10%. All together, these features may have a strong impact in the early detection of AD.The authors acknowledge funding from project PTDC/AAG-TEC/5400/2014, POCI-01-0145-FEDER-016637, POCI-01-0145-FEDER-007688, and UID/CTM/50025/2019 funded by European funds through FEDER (European Funding or Regional Development) via COMPETE2020—POCI (operational program for internationalization and competitively) by national funding through the National Foundation for Science and Technology, I.P. (FCT-MCTES). Additionally, they are grateful to the project IBEROS, Instituto de Bioingeniería en Red para el Envejecimiento Saludable, POCTEP/0245-BEROS-1-E, PROGRAMA INTERREG 2014-2020 funded through FEDER within the cooperation region of Galiza/Spain and North of Portugal. A.C.M. and F.T.C.M. gratefully acknowledges FCT-MCTES for the financial support (PhD grant reference SFRH/BD/115173/2016 intituled “Nanobiosensing platform based on MIP-SERS for breast cancer exosome characterization and detection” and Post-Doc grant reference SFRH/BPD/97891/2013 intituled “Biomedical devices for easier and quicker screening procedures of the Alzheimer’s). This work is part of the Master Thesis in Micro and Nanotechnology Engineering defended by Marta V. Pereira. at FCT NOVA titled “Fabrication of 3D electrodes for biosensor applications” in December 2018.ACSRepositório Científico do Instituto Politécnico do PortoPereira, Marta V.Marques, Ana C.Oliveira, DanielaMartins, RodrigoMoreira, FelisminaSales, Maria Goreti FerreiraFortunato, Elvira2021-09-27T14:38:35Z2020-052020-05-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.22/18576eng10.1021/acsomega.0c00062info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-03-13T13:09:56Zoai:recipp.ipp.pt:10400.22/18576Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T17:37:55.384443Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Paper-Based Platform with an In Situ Molecularly Imprinted Polymer for β-Amyloid
title Paper-Based Platform with an In Situ Molecularly Imprinted Polymer for β-Amyloid
spellingShingle Paper-Based Platform with an In Situ Molecularly Imprinted Polymer for β-Amyloid
Pereira, Marta V.
Sensors
Peptides and proteins
Electrodes
Biotechnology
Polymers
title_short Paper-Based Platform with an In Situ Molecularly Imprinted Polymer for β-Amyloid
title_full Paper-Based Platform with an In Situ Molecularly Imprinted Polymer for β-Amyloid
title_fullStr Paper-Based Platform with an In Situ Molecularly Imprinted Polymer for β-Amyloid
title_full_unstemmed Paper-Based Platform with an In Situ Molecularly Imprinted Polymer for β-Amyloid
title_sort Paper-Based Platform with an In Situ Molecularly Imprinted Polymer for β-Amyloid
author Pereira, Marta V.
author_facet Pereira, Marta V.
Marques, Ana C.
Oliveira, Daniela
Martins, Rodrigo
Moreira, Felismina
Sales, Maria Goreti Ferreira
Fortunato, Elvira
author_role author
author2 Marques, Ana C.
Oliveira, Daniela
Martins, Rodrigo
Moreira, Felismina
Sales, Maria Goreti Ferreira
Fortunato, Elvira
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Repositório Científico do Instituto Politécnico do Porto
dc.contributor.author.fl_str_mv Pereira, Marta V.
Marques, Ana C.
Oliveira, Daniela
Martins, Rodrigo
Moreira, Felismina
Sales, Maria Goreti Ferreira
Fortunato, Elvira
dc.subject.por.fl_str_mv Sensors
Peptides and proteins
Electrodes
Biotechnology
Polymers
topic Sensors
Peptides and proteins
Electrodes
Biotechnology
Polymers
description Alzheimer’s disease (AD) is one of the most common forms of dementia affecting millions of people worldwide. Currently, an easy and effective form of diagnosis is missing, which significantly hinders a possible improvement of the patient’s quality of life. In this context, biosensors emerge as a future solution, opening the doors for preventive medicine and allowing the premature diagnosis of numerous pathologies. This work presents a pioneering biosensor that combines a bottom-up design approach using paper as a platform for the electrochemical recognition of peptide amyloid β-42 (Aβ-42), a biomarker for AD present in blood, associated with visible differences in the brain tissue and responsible for the formation of senile plaques. The sensor layer relies on a molecularly imprinted polymer as a biorecognition element, created on the carbon ink electrode’s surface by electropolymerizing a mixture of the target analyte (Aβ-42) and a monomer (O-phenylenediamine) at neutral pH 7.2. Next, the template molecule was removed from the polymeric network by enzymatic and acidic treatments. The vacant sites so obtained preserved the shape of the imprinted protein and were able to rebind the target analyte. Morphological and chemical analyses were performed in order to control the surface modification of the materials. The analytical performance of the biosensor was evaluated by an electroanalytical technique, namely, square wave voltammetry. For this purpose, the analytical response of the biosensor was tested with standard solutions ranging from 0.1 ng/mL to 1 μg/mL of Aβ-42. The linear response of the biosensor went down to 0.1 ng/mL. Overall, the developed biosensor offered numerous benefits, such as simplicity, low cost, reproducibility, fast response, and repeatability less than 10%. All together, these features may have a strong impact in the early detection of AD.
publishDate 2020
dc.date.none.fl_str_mv 2020-05
2020-05-01T00:00:00Z
2021-09-27T14:38:35Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10400.22/18576
url http://hdl.handle.net/10400.22/18576
dc.language.iso.fl_str_mv eng
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dc.relation.none.fl_str_mv 10.1021/acsomega.0c00062
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
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dc.publisher.none.fl_str_mv ACS
publisher.none.fl_str_mv ACS
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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