Abstract
Objective: To establish an electrochemical immunosensor for the determination of serum trypsin levels using a multiwall carbon nanotubes (MWCNTs)-composite-modified electrode. Method: A MWCNT composite coated on the surface of bare gold electrodes was used for fixation of an anti-trypsin antibody. The assembly process and the performance indicators, including sensitivity, linear range of detection, anti-jamming performance, and stability, of the electrochemical immunosensor were examined by cyclic voltammetry (CV) and electrochemical impedance spectroscopy (EIS). Results: With optimized experimental conditions, the difference of the current value measured by differential pulse voltammetry (DPV) showed a linear relationship with the concentration of serum trypsin within 0.10–100 ng/mL. The detection limit for trypsin using this sensor was 0.002 ng/mL. Conclusions: The electrochemical immunosensor built using the MWCNT-composite-modified electrode is simple to operate and has a fast response time, along with a wide linear range, high sensitivity, and accuracy, making it suitable for serum trypsin detection.
Highlights
Pancreatic cancer is a common cancer with a high mortality rate
The nano-Au-multiwall carbon nanotubes (MWCNTs)/Poly(diallyldimethylammonium Chloride) (PDDA) composite membrane-covered electrode possessed a pair of reversible redox/oxidation peaks
When the anti-trypsin antibody adsorbed to the surface of the composite membrane, the current decreased
Summary
Pancreatic cancer is a common cancer with a high mortality rate. Due to a lack of early diagnostic and prognostic markers, more than 80% of clinically-confirmed pancreatic cancers are diagnosed in the later stages, limiting the availability of treatment options [1–3]. Diagnosis is the key to improve the prognosis of pancreatic cancer, but there is still a lack of clinically effective non-invasive screening methods. The identification of new serum markers that can facilitate early diagnosis of pancreatic cancer is important. Trypsin is a digestive enzyme that selectively hydrolyzes polypeptide chains of lysine or arginine residues, and participates in the invasion and metastasis of pancreatic cancer by promoting the degradation of the extracellular matrix. Trypsin can activate protease activated receptor 2
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