TY - JOUR
T1 - Novel Approach for Simultaneous Analysis of Peptide Metabolites from Orally Administered Glycinin in Rat Bloodstream by Coumarin-Tagged MALDI-MS
AU - Sheng, Xiaojing
AU - Tanaka, Mitsuru
AU - Katagihara, Risa
AU - Hashimoto, Marika
AU - Nagaoka, Satoshi
AU - Matsui, Toshiro
N1 - Funding Information:
This work was supported by JSPS KAKENHI grant numbers JP20H00570 to S.N. and JP21H04863 to T.M.
Publisher Copyright:
©
PY - 2021/12/15
Y1 - 2021/12/15
N2 - 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 °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.
AB - 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 °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.
UR - http://www.scopus.com/inward/record.url?scp=85120752686&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85120752686&partnerID=8YFLogxK
U2 - 10.1021/acs.jafc.1c05791
DO - 10.1021/acs.jafc.1c05791
M3 - Article
C2 - 34860514
AN - SCOPUS:85120752686
SN - 0021-8561
VL - 69
SP - 14840
EP - 14848
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
IS - 49
ER -