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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Pastrello, Bruna [1] ; dos Santos, Giovanny Carvalho [1] ; da Silva-Filho, Luiz Carlos [1] ; de Souza, Aguinaldo Robinson [1] ; Morgon, Nelson Henrique [2] ; Ximenes, Valdecir Farias [1]
Total Authors: 6
[1] UNESP Sao Paulo State Univ, Fac Sci, Dept Chem, BR-17033360 Bauru, SP - Brazil
[2] Campinas State Univ UNICAMP, Inst Chem, Dept Phys Chem, BR-13083861 Campinas, SP - Brazil
Total Affiliations: 2
Document type: Journal article
Source: DYES AND PIGMENTS; v. 173, FEB 2020.
Web of Science Citations: 1

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 x 10(5) mol(-1) L) and by protein intrinsic fluorescence quenching (5.1 x 10(5) 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 (epsilon = 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. (AU)

FAPESP's process: 15/22338-9 - Study of the interaction between drugs and human serum albumin (HSA) based on computer simulation, DFT and TDDFT, experiments of electronic circular dichroism, ECD, and determination of the bond formation constant
Grantee:Aguinaldo Robinson de Souza
Support type: Regular Research Grants
FAPESP's process: 14/50926-0 - INCT 2014: biodiversity and natural products
Grantee:Vanderlan da Silva Bolzani
Support type: BIOTA-FAPESP Program - Thematic Grants
FAPESP's process: 15/00615-0 - Studies on the synthesis and photochemical and photophysical characterization of quinoline derivatives with donor-p-acceptor structure for use as sensitizing dyes in organic electronic devices
Grantee:Giovanny Carvalho dos Santos
Support type: Scholarships in Brazil - Doctorate
FAPESP's process: 18/14506-7 - Study about the one-pot synthesis and application as organic dyes of quinolone and anthrazoline derivatives
Grantee:Luiz Carlos da Silva Filho
Support type: Regular Research Grants
FAPESP's process: 16/20549-5 - Development and application of fluorescent probes and probes based on circular dichroism for the interaction studies of ligands with protein, characterization of amyloid proteins and determination of enzymatic activity
Grantee:Valdecir Farias Ximenes
Support type: Regular Research Grants