Novel aminoquinoline-based solvatochromic fluorescence probe: Interaction with albumin, lysozyme and characterization of amyloid fibrils

Detalhes bibliográficos
Autor(a) principal: Pastrello, Bruna [UNESP]
Data de Publicação: 2020
Outros Autores: dos Santos, Giovanny Carvalho [UNESP], Silva-Filho, Luiz Carlos da [UNESP], de Souza, Aguinaldo Robinson [UNESP], Morgon, Nelson Henrique, Ximenes, Valdecir Farias [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1016/j.dyepig.2019.107874
http://hdl.handle.net/11449/201177
Resumo: A novel aminoquinoline derivative (AQ) was synthesized and applied as a solvatochromic fluorescent probe to study proteins and their alterations. AQ is not fluorescent in aqueous solution but has its fluorescence quantum yield significantly increased upon binding to albumin. The generation of an induced circular dichroism signal in AQ confirmed the complexation. The Job's plot method revealed an 1:1 stoichiometry for the host-guest complex. The binding constant was determined by AQ fluorescence increase (2.7 × 105 mol−1 L) and by protein intrinsic fluorescence quenching (5.1 × 105 mol−1 L). The displacement of AQ from albumin by warfarin and ibuprofen showed that Sudlow's drug site-I is the preferential binding site. By applying the Bilot-Kawski solvatochromic model to the spectral shifts of fifteen solvents, the microenvironment dielectric constant at albumin site-I was estimated (ε = 14.8). In agreement, the average fluorescence lifetime of AQ complexed with albumin (6.11 ns) was close to dichloromethane (6.53 ns) and acetone (6.34 ns), which have dielectric constants of 8.9 and 21.0, respectively. Albumin was thermically treated to formation of amyloid fibril aggregates. AQ was able to differentiate the altered and native protein. Sodium dodecyl sulfate-induced aggregation of lysozyme to amyloid fibril was also efficiently detected by the AQ fluorescence increase. AQ was as efficient as the chromogenic bromocresol purple in the quantitative analysis of albumin. In conclusion, AQ can be considered a new solvatochromic fluorescent probe with several potential applications.
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spelling Novel aminoquinoline-based solvatochromic fluorescence probe: Interaction with albumin, lysozyme and characterization of amyloid fibrilsAlbuminAminoquinoline derivativeAmyloid fibril aggregatesLysozymeOne-pot synthesisSolvatochromic fluorescent probeA novel aminoquinoline derivative (AQ) was synthesized and applied as a solvatochromic fluorescent probe to study proteins and their alterations. AQ is not fluorescent in aqueous solution but has its fluorescence quantum yield significantly increased upon binding to albumin. The generation of an induced circular dichroism signal in AQ confirmed the complexation. The Job's plot method revealed an 1:1 stoichiometry for the host-guest complex. The binding constant was determined by AQ fluorescence increase (2.7 × 105 mol−1 L) and by protein intrinsic fluorescence quenching (5.1 × 105 mol−1 L). The displacement of AQ from albumin by warfarin and ibuprofen showed that Sudlow's drug site-I is the preferential binding site. By applying the Bilot-Kawski solvatochromic model to the spectral shifts of fifteen solvents, the microenvironment dielectric constant at albumin site-I was estimated (ε = 14.8). In agreement, the average fluorescence lifetime of AQ complexed with albumin (6.11 ns) was close to dichloromethane (6.53 ns) and acetone (6.34 ns), which have dielectric constants of 8.9 and 21.0, respectively. Albumin was thermically treated to formation of amyloid fibril aggregates. AQ was able to differentiate the altered and native protein. Sodium dodecyl sulfate-induced aggregation of lysozyme to amyloid fibril was also efficiently detected by the AQ fluorescence increase. AQ was as efficient as the chromogenic bromocresol purple in the quantitative analysis of albumin. In conclusion, AQ can be considered a new solvatochromic fluorescent probe with several potential applications.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Instituto Nacional de Ciência e Tecnologia em ToxinasDepartment of Chemistry Faculty of Sciences UNESP - São Paulo State UniversityDepartment of Physical Chemistry Institute of Chemistry Campinas State University (UNICAMP)Department of Chemistry Faculty of Sciences UNESP - São Paulo State UniversityFAPESP: 2014/50926-0FAPESP: 2015/00615-0FAPESP: 2015/22338-9FAPESP: 2016/20549-5FAPESP: 2018/14506-7CNPq: 302769/2018-8CNPq: 302793/2016-0CNPq: 305541/2017-0Instituto Nacional de Ciência e Tecnologia em Toxinas: 465637/2014-0Universidade Estadual Paulista (Unesp)Universidade Estadual de Campinas (UNICAMP)Pastrello, Bruna [UNESP]dos Santos, Giovanny Carvalho [UNESP]Silva-Filho, Luiz Carlos da [UNESP]de Souza, Aguinaldo Robinson [UNESP]Morgon, Nelson HenriqueXimenes, Valdecir Farias [UNESP]2020-12-12T02:26:00Z2020-12-12T02:26:00Z2020-02-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1016/j.dyepig.2019.107874Dyes and Pigments, v. 173.1873-37430143-7208http://hdl.handle.net/11449/20117710.1016/j.dyepig.2019.1078742-s2.0-85072061620Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengDyes and Pigmentsinfo:eu-repo/semantics/openAccess2024-04-29T18:16:43Zoai:repositorio.unesp.br:11449/201177Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T13:51:30.845529Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Novel aminoquinoline-based solvatochromic fluorescence probe: Interaction with albumin, lysozyme and characterization of amyloid fibrils
title Novel aminoquinoline-based solvatochromic fluorescence probe: Interaction with albumin, lysozyme and characterization of amyloid fibrils
spellingShingle Novel aminoquinoline-based solvatochromic fluorescence probe: Interaction with albumin, lysozyme and characterization of amyloid fibrils
Pastrello, Bruna [UNESP]
Albumin
Aminoquinoline derivative
Amyloid fibril aggregates
Lysozyme
One-pot synthesis
Solvatochromic fluorescent probe
title_short Novel aminoquinoline-based solvatochromic fluorescence probe: Interaction with albumin, lysozyme and characterization of amyloid fibrils
title_full Novel aminoquinoline-based solvatochromic fluorescence probe: Interaction with albumin, lysozyme and characterization of amyloid fibrils
title_fullStr Novel aminoquinoline-based solvatochromic fluorescence probe: Interaction with albumin, lysozyme and characterization of amyloid fibrils
title_full_unstemmed Novel aminoquinoline-based solvatochromic fluorescence probe: Interaction with albumin, lysozyme and characterization of amyloid fibrils
title_sort Novel aminoquinoline-based solvatochromic fluorescence probe: Interaction with albumin, lysozyme and characterization of amyloid fibrils
author Pastrello, Bruna [UNESP]
author_facet Pastrello, Bruna [UNESP]
dos Santos, Giovanny Carvalho [UNESP]
Silva-Filho, Luiz Carlos da [UNESP]
de Souza, Aguinaldo Robinson [UNESP]
Morgon, Nelson Henrique
Ximenes, Valdecir Farias [UNESP]
author_role author
author2 dos Santos, Giovanny Carvalho [UNESP]
Silva-Filho, Luiz Carlos da [UNESP]
de Souza, Aguinaldo Robinson [UNESP]
Morgon, Nelson Henrique
Ximenes, Valdecir Farias [UNESP]
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
Universidade Estadual de Campinas (UNICAMP)
dc.contributor.author.fl_str_mv Pastrello, Bruna [UNESP]
dos Santos, Giovanny Carvalho [UNESP]
Silva-Filho, Luiz Carlos da [UNESP]
de Souza, Aguinaldo Robinson [UNESP]
Morgon, Nelson Henrique
Ximenes, Valdecir Farias [UNESP]
dc.subject.por.fl_str_mv Albumin
Aminoquinoline derivative
Amyloid fibril aggregates
Lysozyme
One-pot synthesis
Solvatochromic fluorescent probe
topic Albumin
Aminoquinoline derivative
Amyloid fibril aggregates
Lysozyme
One-pot synthesis
Solvatochromic fluorescent probe
description A novel aminoquinoline derivative (AQ) was synthesized and applied as a solvatochromic fluorescent probe to study proteins and their alterations. AQ is not fluorescent in aqueous solution but has its fluorescence quantum yield significantly increased upon binding to albumin. The generation of an induced circular dichroism signal in AQ confirmed the complexation. The Job's plot method revealed an 1:1 stoichiometry for the host-guest complex. The binding constant was determined by AQ fluorescence increase (2.7 × 105 mol−1 L) and by protein intrinsic fluorescence quenching (5.1 × 105 mol−1 L). The displacement of AQ from albumin by warfarin and ibuprofen showed that Sudlow's drug site-I is the preferential binding site. By applying the Bilot-Kawski solvatochromic model to the spectral shifts of fifteen solvents, the microenvironment dielectric constant at albumin site-I was estimated (ε = 14.8). In agreement, the average fluorescence lifetime of AQ complexed with albumin (6.11 ns) was close to dichloromethane (6.53 ns) and acetone (6.34 ns), which have dielectric constants of 8.9 and 21.0, respectively. Albumin was thermically treated to formation of amyloid fibril aggregates. AQ was able to differentiate the altered and native protein. Sodium dodecyl sulfate-induced aggregation of lysozyme to amyloid fibril was also efficiently detected by the AQ fluorescence increase. AQ was as efficient as the chromogenic bromocresol purple in the quantitative analysis of albumin. In conclusion, AQ can be considered a new solvatochromic fluorescent probe with several potential applications.
publishDate 2020
dc.date.none.fl_str_mv 2020-12-12T02:26:00Z
2020-12-12T02:26:00Z
2020-02-01
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.dyepig.2019.107874
Dyes and Pigments, v. 173.
1873-3743
0143-7208
http://hdl.handle.net/11449/201177
10.1016/j.dyepig.2019.107874
2-s2.0-85072061620
url http://dx.doi.org/10.1016/j.dyepig.2019.107874
http://hdl.handle.net/11449/201177
identifier_str_mv Dyes and Pigments, v. 173.
1873-3743
0143-7208
10.1016/j.dyepig.2019.107874
2-s2.0-85072061620
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Dyes and Pigments
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
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