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MoS2/S@g-CN Composite Electrode for L-Tryptophan Sensing
Theophile Niyitanga1, Aarti Pathak2, Archana Chaudhary2,3
1School of Materials Science and Engineering, Yeungnam University, Gyeongsan 38541, Republic of Korea.
Biosensors
|November 24, 2023
Summary
This study introduces a novel electrochemical sensor for detecting L-tryptophan (L-TRP), an essential amino acid. The sensor, utilizing a MoS2/S@g-CN modified electrode, offers a sensitive and stable method for L-TRP quantification.
Area of Science:
- Electrochemistry
- Materials Science
- Analytical Chemistry
Background:
- L-tryptophan (L-TRP) is an essential amino acid crucial for human nitrogen balance.
- Accurate quantification of L-TRP is vital for nutritional and health monitoring.
- Existing detection methods may lack sensitivity, stability, or selectivity.
Purpose of the Study:
- To develop and characterize a novel electrochemical sensor for sensitive L-tryptophan detection.
- To synthesize and analyze a molybdenum disulfide/sulfur-g-carbon nitride (MoS2/S@g-CN) composite.
- To evaluate the performance of the modified electrode for L-TRP quantification.
Main Methods:
- Hydrothermal synthesis of the MoS2/S@g-CN composite.
- Characterization using PXRD, SEM, XPS, and EDX.
- Fabrication of a MoS2/S@g-CN modified glassy carbon electrode (GC).
- Electrochemical detection of L-TRP using cyclic voltammetry (CV) and differential pulse voltammetry (DPV).
Main Results:
- The MoS2/S@g-CN composite exhibited porous ball structures with MoS2 decorated on S@g-CN.
- XPS confirmed the presence of Mo, S, O, C, and N elements.
- The modified electrode achieved a low limit of detection (LoD) of 0.03 µM for L-TRP.
- High sensitivity (1.74 µA/µMcm²), stability, repeatability, and selectivity were demonstrated.
Conclusions:
- The developed MoS2/S@g-CN/GC electrode is a highly effective platform for electrochemical L-TRP detection.
- The sensor offers significant advantages in terms of sensitivity, stability, and selectivity.
- This approach provides a promising tool for quantifying essential amino acids in biological samples.

