BSA-stabilized Au clusters as peroxidase mimetics for use in xanthine detection

Area of Science:

• Nanomaterials
• Biochemistry
• Analytical Chemistry

Background:

• Peroxidase mimetics are crucial for bioanalysis.
• Traditional enzyme mimetics face limitations in stability and biocompatibility.
• Bovine serum albumin (BSA) stabilized gold (Au) clusters offer a promising alternative.

Purpose of the Study:

• To demonstrate the peroxidase-like activity of BSA-Au clusters.
• To develop a colorimetric method for hydrogen peroxide (H2O2) detection.
• To establish a sensitive assay for xanthine detection in biological samples.

Main Methods:

• Synthesis of BSA-Au clusters.
• Characterization of BSA-Au cluster properties (pH, temperature stability).
• Colorimetric detection of H2O2 using 3,3,5,5-tetramethylbenzidine (TMB) substrate.
• Development of a xanthine detection assay using xanthine oxidase (XOD).

Main Results:

• BSA-Au clusters exhibit high intrinsic peroxidase-like activity and robustness.
• A sensitive colorimetric method for H2O2 detection was achieved with a limit of detection of 2.0 × 10(-8)M.
• A sensitive and selective assay for xanthine detection with a detection limit of 5 × 10(-7)M was developed.
• The method was successfully applied to detect xanthine in human urine and serum samples.

Conclusions:

• BSA-Au clusters are highly effective and stable peroxidase mimetics.
• These clusters provide a sensitive and selective platform for H2O2 and xanthine detection.
• The developed methods show potential for practical bioanalytical applications.