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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
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 phosphopr...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9220892/ https://www.ncbi.nlm.nih.gov/pubmed/35735509 http://dx.doi.org/10.3390/bios12060361 |
Sumario: | 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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