Bifunctional Magnetic Fe3O4@Cu2O@TiO2 Nanosphere-Mediated Dual-Mode Assay of PTP1B Activity Based on Photocurrent Polarity Switching and Nanozyme-Engineered Biocatalytic Precipitation Strategies.
Anal Chem
; 94(39): 13342-13349, 2022 10 04.
Article
en En
| MEDLINE
| ID: mdl-36129464
ABSTRACT
Dysregulation of protein phosphatases is associated with the progression of various human diseases and cancers. Herein, a photoelectrochemical (PEC)-quartz crystal microbalance (QCM) dual-mode sensing platform was developed for protein tyrosine phosphatase 1B (PTP1B) activity assay based on bifunctional magnetic Fe3O4@Cu2O@TiO2 nanosphere-mediated PEC photocurrent polarity switching and QCM signal amplification strategies. The PTP1B-specific phosphopeptide (P-peptide) with a cysteine end was designed and immobilized onto the QCM Au chip via the Au-S bond. Subsequently, the Fe3O4@Cu2O@TiO2 nanosphere was connected to the P-peptide via the specific interaction between the phosphate group on the P-peptide and TiO2. After incubation with PTP1B, the dephosphorylation of the P-peptide occurred, causing some Fe3O4@Cu2O@TiO2 nanospheres to be released from the chip surface. The released magnetic Fe3O4@Cu2O@TiO2 nanospheres (labeled as R-Fe3O4@Cu2O@TiO2) were quickly separated via magnetic separation technology and attached to the Bi2S3-decorated magnetic indium-tin oxide (Bi2S3/MITO) electrode by magnetic force, inducing the switch of the photocurrent polarity of the electrode from anodic current (the Bi2S3/MITO electrode) to cathodic current (the R-Fe3O4@Cu2O@TiO2/Bi2S3/MITO electrode). Also, the nondephosphorylated P-peptide linked Fe3O4@Cu2O@TiO2 nanospheres as nanozymes with horseradish peroxidase activity to catalyze the formation of precipitation on the surface of the Au chip, leading to a frequency change of the QCM. Thus, the proposed PEC-QCM dual-mode sensing platform achieved accurate and reliable assay of PTP1B activity because of the different mechanisms and independent signal transductions. In addition, this dual-mode sensing platform can be easily extended for other protein phosphatase activity analysis and shows great potential in the early diagnosis of the protein phosphatase-related diseases and the protein phosphatase-targeted drug discovery.
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Técnicas Biosensibles
/
Nanosferas
Tipo de estudio:
Screening_studies
Límite:
Humans
Idioma:
En
Revista:
Anal Chem
Año:
2022
Tipo del documento:
Article