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首页> 外文期刊>Chemistry: A European journal >Solid-Phase Glycosylation of Peptide Templates and On-Bead MAS-NMR Analysis:Perspectives for Glycopeptide Libraries
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Solid-Phase Glycosylation of Peptide Templates and On-Bead MAS-NMR Analysis:Perspectives for Glycopeptide Libraries

机译：肽模板的固相糖基化和珠上MAS-NMR分析：糖肽库的前景。

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摘要

The efficient solid-phase glycosylation of amino acid side chains (serine (Ser),threonine (Thr),and tyrosine (Tyr) in peptides was demonstrated with a variety of glycosyl trichloroacetimidate donors in high yields and purities.A novel photolabile linker,with no chiral centre,was introduced to facilitate analysis by both matrix-assisted laser desorption ionisation time of flight (MALDI-TOF) mass spectrometry and nanoprobe magic angle spinning (MAS) NMR spectroscopy.Product analysis by nanoprobe MAS NMR spectroscopy,LC-MS and MALDI-TOF mass spectrometry of the glycosylation reactions indicated that the reactivity order of the hydroxy side-chain functions of amino acids in peptides on the solid-phase was Tyr>Ser>Thr.The nearly quantitative glycosylation yields and the efficient on-bead product analysis by nanoprobe MAS NMR spectroscopy have made a truly solid-phase approach for the synthesis and analysis of glycopeptide libraries possible.
机译：用各种高产和高纯度的糖基三氯乙酰亚氨酸供体证明了肽中氨基酸侧链（丝氨酸（Ser），苏氨酸（Thr）和酪氨酸（Tyr））的有效固相糖基化。引入无手性中心，以方便通过基质辅助激光解吸电离飞行时间（MALDI-TOF）质谱和纳米探针魔角旋转（MAS）NMR光谱进行分析。通过纳米探针MAS NMR光谱，LC-MS和糖基化反应的MALDI-TOF质谱表明，固相中肽段氨基酸的氨基酸羟基侧链功能的反应顺序为Tyr> Ser> Thr。几乎定量的糖基化收率和有效的珠上产物纳米探针MAS NMR光谱分析已经为糖肽库的合成和分析提供了一种真正的固相方法。

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