ZIF-8 Metal-Organic Framework Electrochemical Biosensor for the Detection of Protein-Protein Interaction
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1021/acs.chemmater.0c04201 http://hdl.handle.net/11449/205955 |
Resumo: | In this study, a novel label-free electrochemical biosensor based on the zeolitic imidazole framework (ZIF-8) was developed for monitoring protein-protein interactions (PPIs). ZIF-8 was deposited on interdigitated electrodes and employed as a transducing material and simultaneously carried the thioredoxin-1 (Trx-1) protein, followed by the deposition of increased concentrations of the cytoplasmic domain of a disintegrin and metalloproteinase 17 (ADAM17cyto) known as the Trx-1 binding partner. Structural and morphological characterizations were used to validate and verify the formation of ZIF-8. The ZIF-8 crystals showed a rhombic dodecahedral structure with mainly exposed (011) facets, a mean particle size of 205 (±22) nm, and a ZIF-8 film thickness around 61 (±6) nm. The interaction between Trx-1 and ADAM17cyto proteins was analyzed through electrochemical impedance spectroscopy (EIS). The results indicate a linear and inverse relationship between the impedance responses at 0.1 Hz for ADAM17cyto concentrations from 50 nM to 8 μM, with a coefficient of variation from 1.0% to 11.4%. The proposed biosensor also displayed a significant selectivity and stability verified by using ADAM17cyto mutant and BSA as controls. As a proof-of-concept, we compared the results with a widely used type of PPI assay based on antibody recognition, the solid-phase binding assay, using the same proteins. The solid-phase binding assay was able to detect a significant binding only in ADAM17cyto concentrations above 0.5 μM, with a coefficient of variation varying from 5.4% to 27.5%. The results demonstrate that the developed biosensor was 10× more sensitive and reproducible than the conventional solid-phase binding assay. Furthermore, the developed electrochemical biosensor based on ZIF-8 provides a faster, label-free, and low-cost detection analysis, representing a novel strategy in detecting PPIs. |
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ZIF-8 Metal-Organic Framework Electrochemical Biosensor for the Detection of Protein-Protein InteractionIn this study, a novel label-free electrochemical biosensor based on the zeolitic imidazole framework (ZIF-8) was developed for monitoring protein-protein interactions (PPIs). ZIF-8 was deposited on interdigitated electrodes and employed as a transducing material and simultaneously carried the thioredoxin-1 (Trx-1) protein, followed by the deposition of increased concentrations of the cytoplasmic domain of a disintegrin and metalloproteinase 17 (ADAM17cyto) known as the Trx-1 binding partner. Structural and morphological characterizations were used to validate and verify the formation of ZIF-8. The ZIF-8 crystals showed a rhombic dodecahedral structure with mainly exposed (011) facets, a mean particle size of 205 (±22) nm, and a ZIF-8 film thickness around 61 (±6) nm. The interaction between Trx-1 and ADAM17cyto proteins was analyzed through electrochemical impedance spectroscopy (EIS). The results indicate a linear and inverse relationship between the impedance responses at 0.1 Hz for ADAM17cyto concentrations from 50 nM to 8 μM, with a coefficient of variation from 1.0% to 11.4%. The proposed biosensor also displayed a significant selectivity and stability verified by using ADAM17cyto mutant and BSA as controls. As a proof-of-concept, we compared the results with a widely used type of PPI assay based on antibody recognition, the solid-phase binding assay, using the same proteins. The solid-phase binding assay was able to detect a significant binding only in ADAM17cyto concentrations above 0.5 μM, with a coefficient of variation varying from 5.4% to 27.5%. The results demonstrate that the developed biosensor was 10× more sensitive and reproducible than the conventional solid-phase binding assay. Furthermore, the developed electrochemical biosensor based on ZIF-8 provides a faster, label-free, and low-cost detection analysis, representing a novel strategy in detecting PPIs.Laboratório Nacional de Biociências (LNBio) Centro Nacional de Pesquisa em Energia e Materiais (CNPEM)Laboratório Nacional de Nanotecnologia (LNNano) Centro Nacional de Pesquisa em Energia e Materiais (CNPEM)Departamento de Biologia Molecular e Funcional Instituto de Biologia (IB) Universidade de Campinas (UNICAMP)Departamento de Físico-Química Instituto de Química (IQ) Universidade de Campinas (UNICAMP)Programa de Pós Graduação em Ciência e Tecnologia de Materiais (POSMAT) Universidade Estadual Paulista (UNESP)Programa de Pós Graduação em Ciência e Tecnologia de Materiais (POSMAT) Universidade Estadual Paulista (UNESP)Centro Nacional de Pesquisa em Energia e Materiais (CNPEM)Universidade Estadual de Campinas (UNICAMP)Universidade Estadual Paulista (Unesp)Trino, Luciana D.Albano, Luiz G. S.Granato, Daniela C.Santana, Aline G.De Camargo, Davi H. S.Correa, Catia C.Bof Bufon, Carlos C. [UNESP]Paes Leme, Adriana F.2021-06-25T10:24:10Z2021-06-25T10:24:10Z2021-02-23info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article1293-1306http://dx.doi.org/10.1021/acs.chemmater.0c04201Chemistry of Materials, v. 33, n. 4, p. 1293-1306, 2021.1520-50020897-4756http://hdl.handle.net/11449/20595510.1021/acs.chemmater.0c042012-s2.0-85101549708Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengChemistry of Materialsinfo:eu-repo/semantics/openAccess2021-10-22T20:11:26Zoai:repositorio.unesp.br:11449/205955Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T22:05:37.492472Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
ZIF-8 Metal-Organic Framework Electrochemical Biosensor for the Detection of Protein-Protein Interaction |
title |
ZIF-8 Metal-Organic Framework Electrochemical Biosensor for the Detection of Protein-Protein Interaction |
spellingShingle |
ZIF-8 Metal-Organic Framework Electrochemical Biosensor for the Detection of Protein-Protein Interaction Trino, Luciana D. |
title_short |
ZIF-8 Metal-Organic Framework Electrochemical Biosensor for the Detection of Protein-Protein Interaction |
title_full |
ZIF-8 Metal-Organic Framework Electrochemical Biosensor for the Detection of Protein-Protein Interaction |
title_fullStr |
ZIF-8 Metal-Organic Framework Electrochemical Biosensor for the Detection of Protein-Protein Interaction |
title_full_unstemmed |
ZIF-8 Metal-Organic Framework Electrochemical Biosensor for the Detection of Protein-Protein Interaction |
title_sort |
ZIF-8 Metal-Organic Framework Electrochemical Biosensor for the Detection of Protein-Protein Interaction |
author |
Trino, Luciana D. |
author_facet |
Trino, Luciana D. Albano, Luiz G. S. Granato, Daniela C. Santana, Aline G. De Camargo, Davi H. S. Correa, Catia C. Bof Bufon, Carlos C. [UNESP] Paes Leme, Adriana F. |
author_role |
author |
author2 |
Albano, Luiz G. S. Granato, Daniela C. Santana, Aline G. De Camargo, Davi H. S. Correa, Catia C. Bof Bufon, Carlos C. [UNESP] Paes Leme, Adriana F. |
author2_role |
author author author author author author author |
dc.contributor.none.fl_str_mv |
Centro Nacional de Pesquisa em Energia e Materiais (CNPEM) Universidade Estadual de Campinas (UNICAMP) Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Trino, Luciana D. Albano, Luiz G. S. Granato, Daniela C. Santana, Aline G. De Camargo, Davi H. S. Correa, Catia C. Bof Bufon, Carlos C. [UNESP] Paes Leme, Adriana F. |
description |
In this study, a novel label-free electrochemical biosensor based on the zeolitic imidazole framework (ZIF-8) was developed for monitoring protein-protein interactions (PPIs). ZIF-8 was deposited on interdigitated electrodes and employed as a transducing material and simultaneously carried the thioredoxin-1 (Trx-1) protein, followed by the deposition of increased concentrations of the cytoplasmic domain of a disintegrin and metalloproteinase 17 (ADAM17cyto) known as the Trx-1 binding partner. Structural and morphological characterizations were used to validate and verify the formation of ZIF-8. The ZIF-8 crystals showed a rhombic dodecahedral structure with mainly exposed (011) facets, a mean particle size of 205 (±22) nm, and a ZIF-8 film thickness around 61 (±6) nm. The interaction between Trx-1 and ADAM17cyto proteins was analyzed through electrochemical impedance spectroscopy (EIS). The results indicate a linear and inverse relationship between the impedance responses at 0.1 Hz for ADAM17cyto concentrations from 50 nM to 8 μM, with a coefficient of variation from 1.0% to 11.4%. The proposed biosensor also displayed a significant selectivity and stability verified by using ADAM17cyto mutant and BSA as controls. As a proof-of-concept, we compared the results with a widely used type of PPI assay based on antibody recognition, the solid-phase binding assay, using the same proteins. The solid-phase binding assay was able to detect a significant binding only in ADAM17cyto concentrations above 0.5 μM, with a coefficient of variation varying from 5.4% to 27.5%. The results demonstrate that the developed biosensor was 10× more sensitive and reproducible than the conventional solid-phase binding assay. Furthermore, the developed electrochemical biosensor based on ZIF-8 provides a faster, label-free, and low-cost detection analysis, representing a novel strategy in detecting PPIs. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-06-25T10:24:10Z 2021-06-25T10:24:10Z 2021-02-23 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1021/acs.chemmater.0c04201 Chemistry of Materials, v. 33, n. 4, p. 1293-1306, 2021. 1520-5002 0897-4756 http://hdl.handle.net/11449/205955 10.1021/acs.chemmater.0c04201 2-s2.0-85101549708 |
url |
http://dx.doi.org/10.1021/acs.chemmater.0c04201 http://hdl.handle.net/11449/205955 |
identifier_str_mv |
Chemistry of Materials, v. 33, n. 4, p. 1293-1306, 2021. 1520-5002 0897-4756 10.1021/acs.chemmater.0c04201 2-s2.0-85101549708 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Chemistry of Materials |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
1293-1306 |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808129391591424000 |