Predicting the Retention Behavior of Specific O-Linked Glycopeptides.
Predicting the Retention Behavior of Specific O-Linked Glycopeptides.
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DOI：
10.7171/jbt.17-2803-003
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发表时间：
2017-09-01
期刊：
影响因子：
--
通讯作者：
Orlando, Ron
中科院分区：
文献类型：
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作者：
Badgett, Majors J;Boyes, Barry;Orlando, Ron
O-连接糖基化是一种常见的翻译后修饰，可以改变蛋白质的整体结构、极性和功能。反相 (RP) 色谱法是分析 O-糖基化肽及其未修饰对应物的最常见色谱方法，尽管这种方法通常无法充分分离这两种物质。亲水相互作用液相色谱 (HILIC) 可以解决这个问题，因为极性聚糖与极性固定相相互作用，并可能提供从其修饰形式解析肽的能力。在本文中，HILIC 用于将添加有 O-N-乙酰半乳糖胺 (O-GalNAc)、O-N-乙酰氨基葡萄糖 (O-GlcNAc) 和 O-岩藻糖的肽与其天然形式分离，并使用线性回归分析导出代表亲水性程度的系数，作为预测经过这些修饰的肽的保留时间的方法。
O-Linked glycosylation is a common post-translational modification that can alter the overall structure, polarity, and function of proteins. Reverse-phase (RP) chromatography is the most common chromatographic approach to analyze O-glycosylated peptides and their unmodified counterparts, even though this approach often does not provide adequate separation of these two species. Hydrophilic interaction liquid chromatography (HILIC) can be a solution to this problem, as the polar glycan interacts with the polar stationary phase and potentially offers the ability to resolve the peptide from its modified form(s). In this paper, HILIC is used to separate peptides with O-N-acetylgalactosamine (O-GalNAc), O-N-acetylglucosamine (O-GlcNAc), and O-fucose additions from their native forms, and coefficients representing the extent of hydrophilicity were derived using linear regression analysis as a means to predict the retention times of peptides with these modifications.