Recognition of urinary N-linked glycopeptides in kidney cancer patients by hydrophilic carbohydrate functionalized magne
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ORIGINAL PAPER
Recognition of urinary N-linked glycopeptides in kidney cancer patients by hydrophilic carbohydrate functionalized magnetic metal organic framework combined with LC-MS/MS Xufang Hu 1 & Yonglei Wu 1 & Chunhui Deng 1 Received: 4 August 2020 / Accepted: 7 October 2020 # Springer-Verlag GmbH Austria, part of Springer Nature 2020
Abstract A hydrophilic carbohydrate functionalized magnetic metal organic framework (Mag Zr-MOF@G6P) was synthesized via a facile one-step modification strategy for selective glycopeptide capture in virtue of hydrophilic interaction chromatography technique. The inherently hydrophilic Zr-MOF layer not only provides selective size-sieving pore structures but also offers large specific surface area to afford abundant affinity sites. Hydroxyl-rich glucose-6-phosphate was immobilized onto the Zr-MOF via a straightforward coordination manner to regulate its surface property, for the purpose of enhancing its hydrophilicity. Benefitting from the merits of Zr-MOF and glucose-6-phosphate, the as-designed composite exhibits good selectivity (the mass ratio of HRP digests to BSA digests was up to1:200) and low limit of detection (0.1 fmol μL−1) towards the recognition of glycopeptides from standard samples. More excitingly, glycopeptides in urine of healthy people and patients with kidney cancer were successfully enriched and identified by the combined liquid chromatography-mass spectrometry/mass spectrometry technology (LC-MS/MS). Further gene ontology analysis of molecular function and biological process revealed that 13 original glycoproteins of the identified glycopeptides from urine of patients significantly participate in diverse cancer-associated events, including collagen binding, immunoglobulin receptor binding, antigen binding, and complement activation process. Keywords Glycosylation . Post-translational modification . Human urine . Magnetic nanomaterials . Post-functionalization
Introduction Protein glycosylation, as a ubiquitous glycoproteins function and metabolic pathway, profoundly impacts numerous cellular processes and biological events [1]. Rapid accumulating researches have proved that the aberrant glycosylation of proteins results in a series of human diseases such as pulmonary diseases, neurodegenerative and blood disorders, and even cancers [2, 3]. Therefore, the precise and comprehensive analysis of glycosylation is an important premise for discovering Electronic supplementary material The online version of this article (https://doi.org/10.1007/s00604-020-04595-y) contains supplementary material, which is available to authorized users. * Chunhui Deng [email protected] 1
Department of Chemistry, Department of Gastroenterology and Hepatology, Zhongshan Hospital, Institutes of Biomedical Sciences, Fudan University, 200433 Shanghai, China
novel disease biomarkers, revealing disease mechanisms, and making early medical diagnosis. Body fluids including serum, saliva, urine, sweat, and so on have been regarded as significant sources of glycoproteomic research [4–6].
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