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

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Autor(es): dc.contributorUniversidade Estadual Paulista (Unesp)-
Autor(es): dc.contributorUniversidade Estadual de Campinas (UNICAMP)-
Autor(es): dc.creatorPastrello, Bruna [UNESP]-
Autor(es): dc.creatordos Santos, Giovanny Carvalho [UNESP]-
Autor(es): dc.creatorSilva-Filho, Luiz Carlos da [UNESP]-
Autor(es): dc.creatorde Souza, Aguinaldo Robinson [UNESP]-
Autor(es): dc.creatorMorgon, Nelson Henrique-
Autor(es): dc.creatorXimenes, Valdecir Farias [UNESP]-
Data de aceite: dc.date.accessioned2022-02-22T00:32:49Z-
Data de disponibilização: dc.date.available2022-02-22T00:32:49Z-
Data de envio: dc.date.issued2020-12-11-
Data de envio: dc.date.issued2020-12-11-
Data de envio: dc.date.issued2020-01-31-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.dyepig.2019.107874-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/201177-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/201177-
Descrição: dc.descriptionA 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.-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionInstituto Nacional de Ciência e Tecnologia em Toxinas-
Descrição: dc.descriptionDepartment of Chemistry Faculty of Sciences UNESP - São Paulo State University-
Descrição: dc.descriptionDepartment of Physical Chemistry Institute of Chemistry Campinas State University (UNICAMP)-
Descrição: dc.descriptionDepartment of Chemistry Faculty of Sciences UNESP - São Paulo State University-
Descrição: dc.descriptionFAPESP: 2014/50926-0-
Descrição: dc.descriptionFAPESP: 2015/00615-0-
Descrição: dc.descriptionFAPESP: 2015/22338-9-
Descrição: dc.descriptionFAPESP: 2016/20549-5-
Descrição: dc.descriptionFAPESP: 2018/14506-7-
Descrição: dc.descriptionCNPq: 302769/2018-8-
Descrição: dc.descriptionCNPq: 302793/2016-0-
Descrição: dc.descriptionCNPq: 305541/2017-0-
Descrição: dc.descriptionInstituto Nacional de Ciência e Tecnologia em Toxinas: 465637/2014-0-
Idioma: dc.languageen-
Relação: dc.relationDyes and Pigments-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectAlbumin-
Palavras-chave: dc.subjectAminoquinoline derivative-
Palavras-chave: dc.subjectAmyloid fibril aggregates-
Palavras-chave: dc.subjectLysozyme-
Palavras-chave: dc.subjectOne-pot synthesis-
Palavras-chave: dc.subjectSolvatochromic fluorescent probe-
Título: dc.titleNovel aminoquinoline-based solvatochromic fluorescence probe: Interaction with albumin, lysozyme and characterization of amyloid fibrils-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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