Unknown

Dataset Information

0

Phosphoprotein Detection in Sweat Realized by Intercalation Structure 2D@3D g-C3N4@Fe3O4 Wearable Sensitive Motif


ABSTRACT: Abnormal protein phosphorylation in sweat metabolites is closely related to cancer, cardiovascular disease, and other diseases. The real-time monitoring of phosphoproteins in sweat is significant for early monitoring of disease biomarkers. Here, a high-efficiency electrochemical sensor for phosphoprotein in sweat was realized by 2D@3D g-C3N4@Fe3O4 with intercalation structure. Common phosphoprotein β-Casein was selected to demonstrate the platform’s functionalities. The detection limit of g-C3N4@Fe3O4 could be as low as 9.7 μM, and the detection range was from 0.01 mg/mL to 1 mg/mL. In addition, the sensing platform showed good selectivity, reproducibility, and stability. We also investigated the effects of interface structure on adsorption properties and electronic properties of the g-C3N4 and Fe3O4 heterostructure using DFT. More electrons from Fe3O4 were transferred to g-C3N4, which increased the electrons in the energy band of N atoms and promoted the formation of stable N-H bonds with H atoms in phosphoproteins. We demonstrated phosphoprotein sensor functionality by measuring the phosphoprotein in human sweat during exercising. This work realizes a sensing platform for noninvasive and continuous detection of sweat phosphoproteins in wearable devices.

SUBMITTER: Qiao Y 

PROVIDER: S-EPMC9220892 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC9599406 | biostudies-literature
| S-EPMC7331702 | biostudies-literature
| S-EPMC10959519 | biostudies-literature
| S-EPMC6434865 | biostudies-literature
| S-EPMC7876776 | biostudies-literature
| S-EPMC7375234 | biostudies-literature
| S-EPMC9953546 | biostudies-literature
| S-EPMC9131736 | biostudies-literature
| S-EPMC10375429 | biostudies-literature
| S-EPMC9059760 | biostudies-literature