Luminescent imaging of insulin amyloid aggregation using a sensitive ruthenium-based probe in the red region
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/10.1016/j.jinorgbio.2021.111585 http://hdl.handle.net/11449/222276 |
Resumo: | A sensitive and selective strategy to identify insulin fibrils remains a challenge for researchers in amyloid protein research. Thus, it is critical to detect, in vitro, the species generated during amyloid aggregation, particularly the fibrillar species. Here we demonstrate that the luminescent complex cis-[Ru(phen)2(3,4Apy)2]2+ (RuApy; phen = 1,10-phenanthroline; 3,4Apy = 3,4-diaminopyridine) is a rapid, low-cost alternative to in vitro detection of fibrillar insulin, using conventional optical techniques. The RuApy complex displays emission intensity enhancement at 655 nm when associated with insulin, which enables imaging of the conformational changes of the protein's self-aggregation. The complex shows high sensitivity to fibrillar insulin with a limit of detection of 0.85 μM and binding affinity of 12.40 ± 1.84 μM which is comparable to those of Thioflavin T and Congo red, with the advantage of minimizing background fluorescence, absorption of light by biomolecules, and light scattering from physiologic salts in the medium. |
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Luminescent imaging of insulin amyloid aggregation using a sensitive ruthenium-based probe in the red regionAmyloid proteinsFluorescence microscopyFluorescent probesInsulinRuthenium complexesA sensitive and selective strategy to identify insulin fibrils remains a challenge for researchers in amyloid protein research. Thus, it is critical to detect, in vitro, the species generated during amyloid aggregation, particularly the fibrillar species. Here we demonstrate that the luminescent complex cis-[Ru(phen)2(3,4Apy)2]2+ (RuApy; phen = 1,10-phenanthroline; 3,4Apy = 3,4-diaminopyridine) is a rapid, low-cost alternative to in vitro detection of fibrillar insulin, using conventional optical techniques. The RuApy complex displays emission intensity enhancement at 655 nm when associated with insulin, which enables imaging of the conformational changes of the protein's self-aggregation. The complex shows high sensitivity to fibrillar insulin with a limit of detection of 0.85 μM and binding affinity of 12.40 ± 1.84 μM which is comparable to those of Thioflavin T and Congo red, with the advantage of minimizing background fluorescence, absorption of light by biomolecules, and light scattering from physiologic salts in the medium.Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Department of Chemistry Universidade Federal de São Carlos, São CarlosDepartment of Physics Universidade Estadual Paulista, Presidente PrudenteDepartment of Physics Universidade Estadual Paulista, Presidente PrudenteCNPq: 131882/2019-8CNPq: 141137/2019-3CNPq: 166303/2017-8FAPESP: 2017/00839–1FAPESP: 2019/21143–0FAPESP: 2020/12129-1Universidade Federal de São Carlos (UFSCar)Universidade Estadual Paulista (UNESP)Pereira, Lorena M.B.Cali, Mariana P.Marchi, Rafael C.Pazin, Wallance M. [UNESP]Carlos, Rose M.2022-04-28T19:43:41Z2022-04-28T19:43:41Z2021-11-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1016/j.jinorgbio.2021.111585Journal of Inorganic Biochemistry, v. 224.1873-33440162-0134http://hdl.handle.net/11449/22227610.1016/j.jinorgbio.2021.1115852-s2.0-85113411292Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal of Inorganic Biochemistryinfo:eu-repo/semantics/openAccess2022-04-28T19:43:41Zoai:repositorio.unesp.br:11449/222276Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462022-04-28T19:43:41Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Luminescent imaging of insulin amyloid aggregation using a sensitive ruthenium-based probe in the red region |
title |
Luminescent imaging of insulin amyloid aggregation using a sensitive ruthenium-based probe in the red region |
spellingShingle |
Luminescent imaging of insulin amyloid aggregation using a sensitive ruthenium-based probe in the red region Pereira, Lorena M.B. Amyloid proteins Fluorescence microscopy Fluorescent probes Insulin Ruthenium complexes |
title_short |
Luminescent imaging of insulin amyloid aggregation using a sensitive ruthenium-based probe in the red region |
title_full |
Luminescent imaging of insulin amyloid aggregation using a sensitive ruthenium-based probe in the red region |
title_fullStr |
Luminescent imaging of insulin amyloid aggregation using a sensitive ruthenium-based probe in the red region |
title_full_unstemmed |
Luminescent imaging of insulin amyloid aggregation using a sensitive ruthenium-based probe in the red region |
title_sort |
Luminescent imaging of insulin amyloid aggregation using a sensitive ruthenium-based probe in the red region |
author |
Pereira, Lorena M.B. |
author_facet |
Pereira, Lorena M.B. Cali, Mariana P. Marchi, Rafael C. Pazin, Wallance M. [UNESP] Carlos, Rose M. |
author_role |
author |
author2 |
Cali, Mariana P. Marchi, Rafael C. Pazin, Wallance M. [UNESP] Carlos, Rose M. |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Universidade Federal de São Carlos (UFSCar) Universidade Estadual Paulista (UNESP) |
dc.contributor.author.fl_str_mv |
Pereira, Lorena M.B. Cali, Mariana P. Marchi, Rafael C. Pazin, Wallance M. [UNESP] Carlos, Rose M. |
dc.subject.por.fl_str_mv |
Amyloid proteins Fluorescence microscopy Fluorescent probes Insulin Ruthenium complexes |
topic |
Amyloid proteins Fluorescence microscopy Fluorescent probes Insulin Ruthenium complexes |
description |
A sensitive and selective strategy to identify insulin fibrils remains a challenge for researchers in amyloid protein research. Thus, it is critical to detect, in vitro, the species generated during amyloid aggregation, particularly the fibrillar species. Here we demonstrate that the luminescent complex cis-[Ru(phen)2(3,4Apy)2]2+ (RuApy; phen = 1,10-phenanthroline; 3,4Apy = 3,4-diaminopyridine) is a rapid, low-cost alternative to in vitro detection of fibrillar insulin, using conventional optical techniques. The RuApy complex displays emission intensity enhancement at 655 nm when associated with insulin, which enables imaging of the conformational changes of the protein's self-aggregation. The complex shows high sensitivity to fibrillar insulin with a limit of detection of 0.85 μM and binding affinity of 12.40 ± 1.84 μM which is comparable to those of Thioflavin T and Congo red, with the advantage of minimizing background fluorescence, absorption of light by biomolecules, and light scattering from physiologic salts in the medium. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-11-01 2022-04-28T19:43:41Z 2022-04-28T19:43:41Z |
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/10.1016/j.jinorgbio.2021.111585 Journal of Inorganic Biochemistry, v. 224. 1873-3344 0162-0134 http://hdl.handle.net/11449/222276 10.1016/j.jinorgbio.2021.111585 2-s2.0-85113411292 |
url |
http://dx.doi.org/10.1016/j.jinorgbio.2021.111585 http://hdl.handle.net/11449/222276 |
identifier_str_mv |
Journal of Inorganic Biochemistry, v. 224. 1873-3344 0162-0134 10.1016/j.jinorgbio.2021.111585 2-s2.0-85113411292 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Journal of Inorganic Biochemistry |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
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_ |
1797789547163025408 |