期刊
ANALYTICAL CHEMISTRY
卷 91, 期 7, 页码 4852-4859出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.9b00542
关键词
-
资金
- National Natural Science Foundation of China [21675156, 21375125, 21725506, 91543201]
- Instrument Developing Project of the Chinese Academy of Sciences [YZ201503]
- CAS Key Laboratory Foundation of Separation Science for Analytical Chemistry
- National Key R&D Program of China [2017YFA0505003]
- Innovation Program of Science and Research from the Dalian Institute of Chemical Physics [DICP TMSR201601]
Glycopeptidome profiling provides large-scale information about the glycosylation level of endogenous peptides, reflecting the dynamic processes of disease occurrences and developments. However, endogenous glycopeptides are usually submerged in complex fluids containing a wide variety of interference molecules, such as high concentration proteins, nonglycopeptides, and salts, which confounds attempts to identify glycopeptidome. Here, a dual hydrophilic metal organic framework is developed to selectively capture endogenous glycopeptides in complex biological fluid. The hydrophilic matrix material provides specific selectivity toward glycopeptides, while the deliberate surface regulation using hydrophilic species enhances its interaction with glycopeptides. This hydrophilic probe presents an extremely high performance in anti-interfering enrichment of glycopeptides from mimic complex samples, even when the molar ratio of immunoglobulin G versus bovine serum albumin was up to about 1:5000. More excitingly, in the practical application of glycopeptidome analysis, a total of 380 endogenous N-glycopeptides with 180 unique N-glycopeptide sites were identified from human plasma. This strategy is expected to broaden the application of dual-hydrophilic MOF-based materials, especially in dealing with the challenges of extremely complex biological samples.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据