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首页> 外文期刊>Journal of mass spectrometry: JMS >Mass spectrometric study of gas-phase ions of acid beta-glucosidase (Cerezyme) and iminosugar pharmacological chaperones
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Mass spectrometric study of gas-phase ions of acid beta-glucosidase (Cerezyme) and iminosugar pharmacological chaperones

机译：酸性β-葡萄糖苷酶（Cerezyme）和亚氨基糖药理伴侣的气相离子的质谱研究

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摘要

The effect on the conformations and stability of gas-phase ions of Cerezyme, a glycoprotein, when bound to three small-molecule chaperones has been studied using intact ESI MS, collision cross section and MS/MS measurements. To distinguish between the peaks from apo and small-molecule complex ions, Cerezyme is deglycosylated (dg-Cer). ESI MS of dg-Cer reveals that glycosylation accounts for 8.5% of the molecular weight. When excess chaperone, either covalent (2FGF) or noncovalent (A and B iminosugars), is added to solutions of dg-Cer, mass spectra show peaks from 1:1 chaperone-enzyme complexes as well as free enzyme. On average, ions of the apoenzyme have 1.6 times higher cross sections when activated in the source region of the mass spectrometer. For a given charge state, ions of complexes of 2FGF and B have about 30% and 8.4% lower cross sections, respectively, compared to the apoenzyme. Thus, binding the chaperones causes the gas-phase protein to adopt more compact conformations. The noncovalent complex ions dissociate by the loss of charged chaperones. In the gas phase, the relative stability of dg-Cer with B is higher than that with the A, whereas in solution A binds enzyme more strongly than B. Nevertheless, the disagreement is explained based on the greater number of contacts between the B and dg-Cer than the A and dg-Cer (13 vs. 8), indicating the importance of noncovalent interactions within the protein-chaperone complex in the absence of solvent. Findings in this work suggest a hypothesis towards predicting a consistent correlation between gas-phase properties to solution binding properties. Copyright (c) 2014 John Wiley & Sons, Ltd.
机译：使用完整的ESI MS，碰撞截面和MS / MS测量研究了糖蛋白Cerezyme气相离子与三个小分子伴侣结合时对构象和稳定性的影响。为了区分载脂蛋白和小分子复合离子的峰，对Cerezyme进行了去糖基化（dg-Cer）。 dg-Cer的ESI MS显示糖基化占分子量的8.5％。当将过量的共价（2FGF）或非共价（A和B亚氨基糖）伴侣加入到dg-Cer溶液中时，质谱显示出1：1伴侣-酶复合物以及游离酶的峰。平均而言，脱辅酶的离子在质谱仪的源区中被激活时具有1.6倍高的横截面。对于给定的电荷状态，与脱辅酶相比，2FGF和B的复合物离子的横截面分别低约30％和8.4％。因此，结合分子伴侣导致气相蛋白采取更紧密的构象。非共价络合物离子通过带电荷伴侣的损失而解离。在气相中，dg-Cer与B的相对稳定性高于与A的相对稳定性，而在溶液A中的酶与B的结合强度更高。尽管如此，基于B与C之间更多的接触数量来解释分歧。 dg-Cer高于A和dg-Cer（13对8），表明在不存在溶剂的情况下，蛋白质-分子伴侣复合物中非共价相互作用的重要性。这项工作的发现提出了一种假设，即预测气相性质与溶液结合性质之间的一致性相关性。版权所有（c）2014 John Wiley＆Sons，Ltd.

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