Multi-histidine functionalized material for the specific enrichment of sialylated glycopeptides
Multi-histidine functionalized material for the specific enrichment of sialylated glycopeptides
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用于特异性富集唾液酸化糖肽的多组氨酸功能化材料
DOI：
10.1016/j.chroma.2020.461422
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发表时间：
2020
影响因子：
4.1
通讯作者：
Ye Mingliang
中科院分区：
文献类型：
--
作者：
Wang Shuyue;Qin Hongqiang;Dong Jing;Hu Lianghai;Ye Mingliang
唾液酸化是糖基化的一种重要形式，参与多种生物学过程，在疾病的发生发展中起着重要作用。然而，由于各种糖基化之间的丰度低，缺乏高特异性的高效富集方法，唾液酸化的研究仍然是一个挑战。本文合成了多组氨酸修饰的微球（MHM），用于富集唾液酸化糖肽。结果表明，MHM对唾液酸化糖肽的富集能力是非唾液酸化糖肽的100倍以上，表明MHM对唾液酸化糖肽具有良好的富集特异性。将MHM用于大规模蛋白质唾液酸化分析，从4 μL人血清中鉴定出510个完整的糖肽，唾液酸化糖肽特异性超过94.5%。这种良好的特异性可归因于静电相互作用和亲水相互作用的协同效应。因此，MHM可以提供一种替代的方法，从复杂的生物样品的蛋白质组水平上的位点特异性唾液酸化的分析。
Sialylation, an important form of glycosylation, is involved in many biological processes and plays an important role in the development of diseases. However, due to the low abundance among various glycosylation and lack of efficient enrichment method with high specificity, the study of sialylation remains a challenge. Herein, multi-histidine modified microspheres (MHM) were synthesized to enrich sialylated glycopeptides. It was found that MHM could selectively enrich sialylated glycopeptides from over 100 times of non-sialylated glycopeptides, which indicated MHM possessed good enrichment specificity towards sialylated glycopeptides. Furthermore, MHM were utilized to the large-scale analysis of protein sialylation, and 510 intact glycopeptides were identified with over 94.5% sialylated glycopeptide specificity from 4 μL human serum. The good specificity could be attributed to the synergistic effect by the electrostatic interaction and hydrophilic interaction. Hence, MHM could provide an alternative approach for the analysis of site-specific sialylation at proteome level from complex biological samples.