Characterization of impurities in a synthetic renin substrate peptide by fast-atom bombardment mass spectrometry and hybrid tandem mass spectrometry.
Characterization of impurities in a synthetic renin substrate peptide by fast-atom bombardment mass spectrometry and hybrid tandem mass spectrometry.
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DOI：
10.1002/rcm.1290030912
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发表时间：
1989-09-01
期刊：
影响因子：
--
通讯作者：
Gaskell, S J
中科院分区：
文献类型：
--
作者：
Mathews, W R;Runge, T A;Gaskell, S J
合成的肾素底物十肽（Pro-His-Pro-Phe-His-Leu-Val-Ile-His-D-Lys）的快原子轰击质谱表明存在几种副产物，包括质量高12 Da的组分。低能量碰撞活化分解分析使用混合串联仪器进行，并证明，较重的副产物有两个组件，其中的结构修饰是在N-或C-末端。对N-乙酰基衍生物的其他分析表明，对于每种组分，结构修饰阻断了N-乙酰化位点。据认为，这些副产物的形成是由于在去除组氨酸保护基（苄氧基甲基）的过程中产生甲醛，其与肽的N-末端反应以得到咪唑烷酮结构或与D-赖氨酸ε-胺基反应以产生亚胺。虽然副产物的确切成因仍然是推测性的，但很明显，衍生化和串联质谱的组合策略已经允许关于等压混合物的各个组分的结构结论。
Fast-atom bombardment mass spectrometry of a synthetic renin substrate decapeptide (Pro-His-Pro-Phe-His-Leu-Val-Ile-His-D-Lys) indicated the presence of several side-products, including a component 12 Da higher in mass. Low-energy collisionally activated decomposition analyses were performed using a hybrid tandem instrument and demonstrated that the heavier side product had two components, in which the structural modification was either at the N- or the C-terminus. Additional analyses of the N-acetyl derivative indicated that for each component the structural modification blocked a site of N-acetylation. It is suggested that the formation of these side products is attributable to the generation of formaldehyde, during removal of the histidine protecting group (benzyloxymethyl), which reacts with the N-terminus of the peptide to give an imidazolidinone structure or with the D-lysine epsilon-amine group to yield an imine. While the precise genesis of the side-products remains speculative, it is clear that the combined strategy of derivatization and tandem mass spectrometry has allowed structural conclusions concerning individual components of an isobaric mixture.