Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 69, Issue 49, Pages 14840-14848Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.1c05791
Keywords
peptide; metabolite; coumarin derivatization; MALDI-MS; glycinin
Funding
- JSPS KAKENHI [JP20H00570, JP21H04863]
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The study established a novel analytical assay for peptide metabolites from glycinin, using MALDI-MS combined with amine derivatization with coumarin. The use of coumarin derivatization under specific conditions led to improved MS detection of peptides, allowing for successful characterization of glycinin-derived metabolites in rats.
The lack of an appropriate analytical approach characterizing metabolites from dietary proteins may prevent further studies that could clarify their health benefits. In this study, we attempted to establish a novel analytical assay of peptide metabolites from glycinin using matrix-assisted laser desorption/ionization-mass spectrometry (MALDI-MS), in combination with the amine derivatization technique with coumarin (Cou). Cou (30 mmol/L) derivatization of peptides under rapid (30 min) and mild (25 degrees C, pH 8.5) conditions caused higher MS detection of the peptides as compared to nonderivatized peptides. In addition, an MS shift of the target by Cou derivatization (+202.0 m/z) can help to easily discriminate peptide metabolites in glycinin-administered blood, by comparing the MALDI-MS spectra of Cou-derivatized plasma with those of preadministered blood. After the oral administration of glycinin (100 mg/kg) to Sprague-Dawley rats, 15 di- to tetrapeptides were successfully characterized as glycinin-derived metabolites, demonstrating that the proposed Cou-tagged MALDI-MS is an appropriate characterization technique for peptide metabolites.
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