AI Article Synopsis
- Monoacylglycerols (MAGs) are crucial in understanding diseases like diabetes, obesity, and cancers, but detecting them has been challenging due to previous complex methods.
- A new method using 3-nitrophenylboronic acid (3-NPB) makes it easier to analyze MAGs in various biological samples through mass spectrometry, allowing for direct and sensitive detection.
- The technique enhances identification by using isotopic labels, reducing background noise, and improving quantification of MAG levels in different tissues and serum, which could further metabolic research on MAG-related illnesses.
Article Abstract
Monoacylglycerols (MAGs) are active mediators involved in multiple biological processes closely related to the pathological development of diabetes, obesity, and cancers. Sensitive and unambiguous detection of MAGs is thus essential; however, previous methods are both indirect and labor-intensive. Herein, we developed a straightforward approach by derivatization of MAGs with 3-nitrophenylboronic acid (3-NPB) for sensitive and selective analysis in cell lysates, tissues, and serums by mass spectrometry (MS). Reaction occurring between boronic acid and cis-diol moiety of MAGs blocked the formation of multiple adduct ions and tuned MAGs to negatively charged carrying species. In addition, the characteristic isotopic distribution of boron specialized the presence of modified MAGs in MS and led to distinctive identification. To eliminate endogenous interferences, we further introduced isotopic labeled d-NPB equivalently premixed with d-NPB to perform MAG derivatization, which resulted in rapid identification of modified MAGs in biofluids by displaying doublet peak characteristics. A comparative quantification approach was thereafter evoluted to reveal the amount variation of MAGs by d-NPB and d-NPB separately derivatized in different pathological tissue and serum samples. The presently developed NPB-based derivatization approach is expected to be essential in the metabolic study of MAG-related diseases.
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| http://dx.doi.org/10.1021/acs.analchem.9b00805 | DOI Listing |
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