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Monoamine oxidase B activatable red fluorescence probe for bioimaging in cells and zebrafish.
Yang, Zhengmin; Zhong, Tiantian; Mo, Qingyuan; He, Jiman; Chong, Jia; Hu, Xianyun; Zhao, Shulin; Qin, Jiangke.
Afiliação
  • Yang Z; State Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources, School of Chemistry and Pharmaceutical Sciences, Guangxi Normal University, Guilin 541004, PR China; Qiannan Medical College for Nationalities, Duyun 558003, PR China.
  • Zhong T; State Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources, School of Chemistry and Pharmaceutical Sciences, Guangxi Normal University, Guilin 541004, PR China.
  • Mo Q; State Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources, School of Chemistry and Pharmaceutical Sciences, Guangxi Normal University, Guilin 541004, PR China.
  • He J; State Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources, School of Chemistry and Pharmaceutical Sciences, Guangxi Normal University, Guilin 541004, PR China.
  • Chong J; Qiannan Medical College for Nationalities, Duyun 558003, PR China.
  • Hu X; Qiannan Medical College for Nationalities, Duyun 558003, PR China.
  • Zhao S; State Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources, School of Chemistry and Pharmaceutical Sciences, Guangxi Normal University, Guilin 541004, PR China.
  • Qin J; State Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources, School of Chemistry and Pharmaceutical Sciences, Guangxi Normal University, Guilin 541004, PR China. Electronic address: jiangkeq@sina.com.
Bioorg Chem ; 145: 107156, 2024 Apr.
Article em En | MEDLINE | ID: mdl-38387393
ABSTRACT
A real-time and specific for the detection of Monoamine Oxidase B (MAO-B) to investigate the MAO-B-relevant disease development and treatment process is urgently desirable. Here, we utilized MAO-B to catalyze the conversion of propylamino groups to aldehyde groups, which was then quickly followed by a ß-elimination process to produce fluorescent probes (FNJP) that may be used to detect MAO-B in vitro and in vivo. The FNJP probe possesses unique properties, including favorable reactivity (Km = 10.8 µM), high cell permeability, and NIR characteristics (λem = 610 nm). Moreover, the FNJP probe showed high selectivity for MAO-B and was able to detect endogenous MAO-B levels from a mixed population of NIH-3 T3 and HepG2 cells. MAO-B expression was found to be increased in cells under lipopolysaccharide-stimulated cellular oxidative stress in neuronal-like SH-SY5Y cells. In addition, the visualization of FNJP for MAO-B activity in zebrafish can be an effective tool for exploring the biofunctions of MAO-B. Considering these excellent properties, the FNJP probe may be a powerful tool for detecting MAO-B levels in living organisms and can be used for accurate clinical diagnoses of related diseases.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Monoaminoxidase / Neuroblastoma Limite: Animals / Humans Idioma: En Revista: Bioorg Chem Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Monoaminoxidase / Neuroblastoma Limite: Animals / Humans Idioma: En Revista: Bioorg Chem Ano de publicação: 2024 Tipo de documento: Article