In-Depth Analysis of Glycoprotein Sialylation in Serum Using a Dual-Functional Material with Superior Hydrophilicity and Switchable Surface Charge
In-Depth Analysis of Glycoprotein Sialylation in Serum Using a Dual-Functional Material with Superior Hydrophilicity and Switchable Surface Charge
复制标题
使用具有优异亲水性和可切换表面电荷的双功能材料深入分析血清中的糖蛋白唾液酸化
DOI：
10.1021/acs.analchem.6b04394
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发表时间：
2017-04-04
影响因子：
7.4
通讯作者：
Liang, Xinmiao
中科院分区：
文献类型：
--
作者：
Dong, Xuefang;Qin, Hongqiang;Liang, Xinmiao
唾液酸化通常发生在聚糖的末端，其畸变通常与包括神经系统疾病和癌症在内的疾病相关。然而，复杂生物样品中糖蛋白唾液酸化的分析由于其低丰度而仍然具有挑战性。本文中，制备了具有亲水相互作用和可切换表面电荷的组氨酸键合的二氧化硅（HBS）材料，以从蛋白质组学样品的消化物中富集唾液酸化糖肽（SGPs）。通过结合上级亲水性和可切换电荷特性，获得了对SGPs的高选择性。在从牛胎球蛋白消化物中富集唾液酸化糖肽的过程中，即使与非唾液酸化糖肽的比例为1：5000，也检测到7种糖肽，证明了使用HBS材料富集SGP的高度特异性。然后，进一步利用HBS材料从人血清的蛋白质消化物中选择性富集SGP，并且仅从2 μ L人血清中鉴定出487个糖位点; 92.0%的糖肽含有至少一个唾液酸，表明通过使用HBS材料进行SGP富集的良好性能。此外，所制备的HBS材料在其他复杂生物样品中糖蛋白唾液酸化的分析中也具有很大的潜在应用。
Sialylation typically occurs at the terminal of glycans, and its aberration often correlates with diseases including neurological diseases and cancer. However, the analysis of glycoprotein sialylation in complex biological samples is still challenging due to their low abundance. Herein, a histidine-bonded silica (HBS) material with a hydrophilic interaction and switchable surface charge was fabricated to enrich sialylated glycopeptides (SGPs) from the digest of proteomics samples. High selectivity toward SGPs was obtained by combining the superior hydrophilicity and switchable-charge characteristics. During the enrichment of sialylated glycopeptides from bovine fetuin digest, seven glycopeptides were detected even at the ratio of 1:5000 with the nonsialylated glycopeptides, demonstrating the high specificity of SGP enrichment by using HBS material. Then, HBS material was further utilized to selectively enrich SGPs from the protein digest of human serum, and 487 glycosites were identified from only 2 mu L of human serum; 92.0% of the glycopeptides contained at least one sialic acid, indicating good performance for SGP enrichment by using HBS material. Furthermore, the prepared HBS material also has great potential applications in the analysis of glycoprotein sialylation from other complex biological samples.