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首页> 外文期刊>The FEBS journal >C-mannosylation in the hypertrehalosaemic hormone from the stick insect Carausius morosus
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C-mannosylation in the hypertrehalosaemic hormone from the stick insect Carausius morosus

机译：棒虫Carausius morosus的高海藻糖激素中的C-甘露糖基化

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摘要

The hypertrehalosaemic hormone from the stick insect Carausius morosus (Cam-HrTH) contains a hexose covalently bound to the ring of the tryptophan, which is in the eighth position in the molecule. We show by solution NMR spectroscopy that the tryptophan is modified at its C-delta 1(C2) by an alpha-mannopyranose. It is the first insect hormone to exhibit C-glycosylation whose exact nature has been determined experimentally. Chemical shift analysis reveals that the unmodified as well as the mannosylated Cam-HrTH are not completely random-coil in aqueous solution. Most prominently, C-mannosylation strongly influences the average orientation of the tryptophan ring in solution and stabilizes it in a position clearly different from that found in the unmodified peptide. NMR diffusion measurements indicate that mannosylation reduces the effective hydrodynamic radius. It induces a change of the average peptide conformation that also diminishes the propensity for aggregation of the peptide.
机译：粘虫Carausius morosus（Cam-HrTH）的高海藻糖原激素含有与色氨酸环共价结合的己糖，后者在分子中的第八位。我们通过溶液NMR光谱表明，色氨酸在其C-δ1（C2）处被α-甘露聚糖修饰。它是第一种具有C-糖基化作用的昆虫激素，其确切性质已通过实验确定。化学位移分析表明，未修饰的以及甘露糖基化的Cam-HrTH在水溶液中不是完全无规卷曲的。最显着的是，C-甘露糖基化强烈影响溶液中色氨酸环的平均方向，并将其稳定在与未修饰肽明显不同的位置。 NMR扩散测量表明，甘露糖基化作用降低了有效流体动力学半径。它引起平均肽构象的改变，这也降低了肽聚集的倾向。

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