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Phosphoprotein Detection in Sweat Realized by Intercalation Structure 2D@3D g-C 3 N 4 @Fe 3 O 4 Wearable Sensitive Motif.

Yuting QiaoLijuan QiaoPeize ZhaoPeng ZhangFanbin WuJiahui ZhangLi GaoBingxin LiuLei Zhang
Published in: Biosensors (2022)
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-C 3 N 4 @Fe 3 O 4 with intercalation structure. Common phosphoprotein β-Casein was selected to demonstrate the platform's functionalities. The detection limit of g-C 3 N 4 @Fe 3 O 4 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-C 3 N 4 and Fe 3 O 4 heterostructure using DFT. More electrons from Fe 3 O 4 were transferred to g-C 3 N 4 , 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.
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