Dual-Readout Tyrosinase Activity Assay Facilitated by a Chromo-Fluorogenic Reaction between Catechols and Naphthoresorcin.
Anal Chem
; 92(2): 2316-2322, 2020 01 21.
Article
em En
| MEDLINE
| ID: mdl-31859491
ABSTRACT
Analyte-responsive chromo-fluorogenic reactions under accessible conditions are important for designing small-molecule spectroscopic probes. We describe a series of newly constructed motifs based on the chromo-fluorogenic reaction between catechol derivatives (typically hydroxytyrosol, dopamine, and levodopa) and naphthoresorcin (NR) in aqueous solution under ambient conditions. The weakly absorptive and fluorogenic catechols/NR was converted to products having visible absorption and bright fluorescence within several minutes. The chromo-fluorophores produced from this reaction had a maximum absorbance at 458 nm and emission at 480 nm with high fluorescence quantum yields (30-84%). Inspired by the tyrosinase-catalyzed hydroxylation of monophenols to catechols, the tyrosinase-enabled chromo-fluorogenic reaction was verified by using monophenol (typically tyrosol) as the substrate. In this regard, a dual-readout tyrosinase activity assay was developed by virtue of the in situ "turn-on" optical signals. Furthermore, a test of tyrosinase inhibition, by using a common inhibitor kojic acid, demonstrated the potential of the chromo-fluorogenic reaction for developing other tyrosinase related assays and signal transduction.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Resorcinóis
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Catecóis
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Monofenol Mono-Oxigenase
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Corantes Fluorescentes
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Naftalenos
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article
País de afiliação:
China