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Quantitation of Alpha-Glucosidase Activity Using Fluorinated Carbohydrate Array and MALDI-TOF-MS
Hyojik Yang1, Allen L Chan1, Vincent LaVallo1
1Department of Chemistry, University of California , Riverside, California 92521, United States.
ACS Applied Materials & Interfaces
|January 14, 2016
Summary
This study introduces a novel method for quantifying alpha-glucosidase (α-GD) activity using mass spectrometry and carbohydrate microarrays. This technique offers improved accuracy by minimizing sample interference, aiding in disease diagnosis.
Area of Science:
- Biochemistry
- Analytical Chemistry
- Biotechnology
Background:
- Quantifying alpha-glucosidase (α-GD) activity is crucial for diagnosing diseases like Pompe disease and type II diabetes.
- Conventional colorimetric assays often face challenges due to matrix interference from biological samples.
Purpose of the Study:
- To develop and validate a new, interference-resistant method for determining α-GD activity.
- To leverage matrix-assisted laser desorption/ionization (MALDI)-time-of-flight (TOF) mass spectrometry (MS) combined with advanced surface chemistry for enzyme activity analysis.
Main Methods:
- Synthesis of carbohydrate probes for capturing enzymatic reaction products.
- Creation of a carbohydrate microarray on a fluorinated gold surface.
- Characterization of the array using MALDI-TOF-MS and analysis of intensity ratios.
Main Results:
- The developed method accurately quantifies α-GD activity.
- The method successfully determined the half maximal inhibitory concentration (IC50) for acarbose and epigallocatechin gallate, aligning with reported values.
- The use of a polyfluorinated surface effectively suppressed matrix interference, a common issue in colorimetric methods.
Conclusions:
- This novel MALDI-TOF-MS based approach provides a robust and sensitive platform for α-GD activity quantitation.
- The method overcomes limitations of traditional assays, offering enhanced diagnostic potential.
- The technique demonstrates versatility by enabling the determination of enzyme inhibitor potencies.
