Dataset Information

Synthesis, Purification, and Mass Spectrometric Characterization of Stable Isotope-Labeled Amadori-Glycated Phospholipids.

ABSTRACT: Nonenzymatic glycation of lipids plays an important role in several physiological and pathological processes, such as normal aging and complications of diabetes mellitus. To develop liquid chromatography coupled with mass spectrometric (LC-MS) methods for accurate analysis of Amadori compound-glycated lipids from biological samples, it is essential to obtain isotope-labeled Amadori-lipid standards. Herein, we report optimized methods for the preparation of six stable isotope-labeled Amadori-glycated lipid standards covering four types of lipids, including [13C6]Amadori-phosphatidyl ethanolamine (PE), -phosphatidyl serine (PS), -LysoPE, and -LysoPS. Optimal conditions for the synthesis and purification of these four types of Amadori-glycated lipids were detailed in this study. LC-MS and LC-UV analyses showed that destination products were highly purified (>95%). Accurate mass and MS/MS fragmentation in both positive- and negative-ion modes further validated the identification of these six synthetic [13C6]Amadori-glycated lipid standards. Successful preparation of these highly purified isotope-labeled standards makes it possible to develop targeted LC-MS/MS methods for accurate analysis of Amadori-glycated phospholipids from biological samples.

SUBMITTER: He X

PROVIDER: S-EPMC6275948 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature

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Synthesis, Purification, and Mass Spectrometric Characterization of Stable Isotope-Labeled Amadori-Glycated Phospholipids.

He Xiaobo X Zhang Qibin Q

ACS omega 20181119 11

Nonenzymatic glycation of lipids plays an important role in several physiological and pathological processes, such as normal aging and complications of diabetes mellitus. To develop liquid chromatography coupled with mass spectrometric (LC-MS) methods for accurate analysis of Amadori compound-glycated lipids from biological samples, it is essential to obtain isotope-labeled Amadori-lipid standards. Herein, we report optimized methods for the preparation of six stable isotope-labeled Amadori-glyc ...[more]

PMID: 30533579

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Project description:To facilitate accurate histone variant and post-translational modification (PTM) quantification via mass spectrometry, we present a library of 93 synthetic peptides using Protein-Aqua™ technology. The library contains 55 peptides representing different modified forms from histone H3 peptides, 23 peptides representing H4 peptides, 5 peptides representing canonical H2A peptides, 8 peptides representing H2A.Z peptides, and peptides for both macroH2A and H2A.X. The PTMs on these peptides include lysine mono- (me1), di- (me2), and tri-methylation (me3); lysine acetylation; arginine me1; serine/threonine phosphorylation; and N-terminal acetylation. The library was subjected to chemical derivatization with propionic anhydride, a widely employed protocol for histone peptide quantification. Subsequently, the detection efficiencies were quantified using mass spectrometry extracted ion chromatograms. The library yields a wide spectrum of detection efficiencies, with more than 1700-fold difference between the peptides with the lowest and highest efficiencies. In this paper, we describe the impact of different modifications on peptide detection efficiencies and provide a resource to correct for detection biases among the 93 histone peptides. In brief, there is no correlation between detection efficiency and molecular weight, hydrophobicity, basicity, or modification type. The same types of modifications may have very different effects on detection efficiencies depending on their positions within a peptide. We also observed antagonistic effects between modifications. In a study of mouse trophoblast stem cells, we utilized the detection efficiencies of the peptide library to correct for histone PTM/variant quantification. For most histone peptides examined, the corrected data did not change the biological conclusions but did alter the relative abundance of these peptides. For a low-abundant histone H2A variant, macroH2A, the corrected data led to a different conclusion than the uncorrected data. The peptide library and detection efficiencies presented here may serve as a resource to facilitate studies in the epigenetics and proteomics fields.

Dataset Information

Synthesis, Purification, and Mass Spectrometric Characterization of Stable Isotope-Labeled Amadori-Glycated Phospholipids.

Publications

Synthesis, Purification, and Mass Spectrometric Characterization of Stable Isotope-Labeled Amadori-Glycated Phospholipids.

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