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Updated: Jun 5, 2026

A Hydrogen-Deuterium Exchange Mass Spectrometry (HDX-MS) Platform for Investigating Peptide Biosynthetic Enzymes
Published on: May 4, 2020
Single drop microextraction coupled with matrix-assisted laser desorption/ionization mass spectrometry for rapid and
Hui-Fen Wu1, Suresh Kumar Kailasa, Chi-Hsien Lin
1Department of Chemistry, National Sun Yat-Sen University, Kaohsiung 80424, Taiwan. hwu@faculty.nsysu.edu.tw
Abstract:
Single drop microextraction (SDME) coupled with matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) has been applied for direct analysis of hydrophobic peptides (valinomycin and gramicidin D) from biological samples (urine and plasma) in high salt solution. The optimal conditions such as selection of extraction solvent, stirring rate, extraction time, effect of salt concentration and matrix-to-analyte ratio were investigated. The limits of detection (LODs) were found to be 73 nM to 170 nM for valinomycin and 96 nM to 5.5 µM for gramicidin D in high salt solution (1.7 M of NaCl) in MALDI-MS. The current approach can enhance the LODs by 11-320-fold for gramicidin D analysis in water, urine and plasma in high salt solution. Furthermore, the current approach has been successfully demonstrated for real-world sample analysis (β-carotene from carrots) by MALDI-MS. The current approach is a rapid, simple and efficient clean-up platform for direct analysis of hydrophobic molecules in biological samples from high salt solution.
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